Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Abbey+Morgan+Pals Proteopedia - User contributions [en] 2026-09-21T02:21:07Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488560 Sandbox Reserved 1697 2021-12-09T04:08:34Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The protein 7KIR is found in the organism Bos taurus, is a a protype member of proteins dealing with inositol signaling. The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> This protein is involved in dephosphorylation of inositol which inhibits inositol signaling in cattle. The metal ions assist in holding the water so that it can attack the phosphate to take it off. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In the protein the substrate is <scene name='89/892740/Ligand_view/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, will be dephosphorylated by the water brought in by the magnesium ions.In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the substrate better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> One of the unique things of this enzyme is its use of metal ions, the <scene name='89/892740/Interact_with_metal_ions/1'>amino acids bond with the metal ions</scene> that then bind with the water. The water attacks the phosphate which causes the inositol to dephosphorylate the substrate as seen in the image to the right. The catalytic amino acids in enzyme are mainly polar which causes the magnesium ions to better bond with them.<br /> [[Image:Pic.png | thumb]]<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488558 Sandbox Reserved 1697 2021-12-09T03:32:24Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The protein 7KIR is found in the organism Bos taurus, is a a protype member of proteins dealing with inositol signaling. The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> This protein is involved in dephosphorylation of inositol which inhibits inositol signaling in cattle. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In the protein the substrate is <scene name='89/892740/Ligand_view/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, will be dephosphorylated by the water brought in by the magnesium ions.In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the substrate better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> One of the unique things of this enzyme is its use of metal ions, the <scene name='89/892740/Interact_with_metal_ions/1'>amino acids bond with the metal ions</scene> that then bind with the water. The water attacks the phosphate which causes the inositol to dephosphorylate the substrate as seen in the image to the right. The catalytic amino acids in enzyme are mainly polar which causes the magnesium ions to better bond with them.<br /> [[Image:Pic.png | thumb]]<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488556 Sandbox Reserved 1697 2021-12-09T03:24:41Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The protein 7KIR is found in the organism Bos taurus, is a a protype member of proteins dealing with inositol signaling. The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> This protein is involved in dephosphorylation of inositol which inhibits inositol signaling in cattle. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In the protein the ligand is <scene name='89/892740/Ligand_view/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, will be dephosphorylated by the water brought in by the magnesium ions.In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> One of the unique things of this enzyme is its use of metal ions, the <scene name='89/892740/Interact_with_metal_ions/1'>amino acids bond with the metal ions</scene> that then bind with the water. The water attacks the phosphate which causes the inositol to dephosphorylate the substrate as seen in the image to the right. The catalytic amino acids in enzyme are mainly polar which causes the magnesium ions to better bond with them.<br /> [[Image:Pic.png | thumb]]<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=File:Pic.png&diff=3488555 File:Pic.png 2021-12-09T03:23:03Z

<p>Abbey Morgan Pals: </p> <hr /> <div></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488554 Sandbox Reserved 1697 2021-12-09T03:20:44Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The protein 7KIR is found in the organism Bos taurus, is a a protype member of proteins dealing with inositol signaling. The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> This protein is involved in dephosphorylation of inositol which inhibits inositol signaling in cattle. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In the protein the ligand is <scene name='89/892740/Ligand_view/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, will be dephosphorylated by the water brought in by the magnesium ions.In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> One of the unique things of this enzyme is its use of metal ions, the <scene name='89/892740/Interact_with_metal_ions/1'>amino acids bond with the metal ions</scene> that then bind with the water. The water attacks the phosphate which causes the inositol to dephosphorylate the substrate. The catalytic amino acids in enzyme are mainly polar which causes the magnesium ions to better bond with them.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488551 Sandbox Reserved 1697 2021-12-09T03:12:09Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The protein 7KIR is found in the organism Bos taurus, is a a protype member of proteins dealing with inositol signaling. The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> This protein is involved in dephosphorylation of inositol which inhibits inositol signaling in cattle. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In the protein the ligand is <scene name='89/892740/Ligand_view/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, will be dephosphorylated by the water brought in by the magnesium ions.In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488545 Sandbox Reserved 1697 2021-12-09T03:04:56Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The protein 7KIR is found in the organism Bos taurus, is a a protype member of proteins dealing with inositol signaling. The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> This protein is involved in dephosphorylation of inositol which inhibits inositol signaling in cattle. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488542 Sandbox Reserved 1697 2021-12-09T03:03:01Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The protein 7KIR is found in the organism Bos taurus, is a a protype member of proteins dealing with inositol signaling. The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488540 Sandbox Reserved 1697 2021-12-09T02:53:40Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol. It wraps around the magnesium ions so that it can better attach to the water and then attack the phosphate on inositol. When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488539 Sandbox Reserved 1697 2021-12-09T02:46:34Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the <scene name='89/892740/Spacefill_7kir/1'>proper shape</scene> so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488538 Sandbox Reserved 1697 2021-12-09T02:44:23Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several <scene name='89/892740/7kir_quaternary_structures/1'>tertiary structures</scene> that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488536 Sandbox Reserved 1697 2021-12-09T02:39:20Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488535 Sandbox Reserved 1697 2021-12-09T02:37:10Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is <scene name='89/892740/1inp/1'>1INP</scene>, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488534 Sandbox Reserved 1697 2021-12-09T02:33:42Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/7kir_catalytic_amino_acids/1'>Text To Be Displayed</scene><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The protein 7KIR is a protype member of proteins that work in inositol signaling, specifically dephosphorylating inositol to stop inositol signaling. The protein that the paper primarily mentions is 1INP, all of the proteins in this family share a motif, DPID X T. The X in the motif means that there can be any amino acid in there, in 1INP it is alanine while in <scene name='89/892740/7kir_catalytic_amino_acids/1'>7KIR</scene> is aspartic acid. The mutation in these proteins have no functional impact on the protein's ability to dephosphorylate inositol. <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488531 Sandbox Reserved 1697 2021-12-09T02:15:27Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape.<br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488529 Sandbox Reserved 1697 2021-12-09T02:08:43Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules.<br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=File:Dephosphorylation_Image.png&diff=3488489 File:Dephosphorylation Image.png 2021-12-09T01:31:08Z

<p>Abbey Morgan Pals: uploaded a new version of "Image:Dephosphorylation Image.png": Shows how protein holds onto magnesium ions that then take phosphate off of IP3.</p> <hr /> <div>Shows how motif holds onto metal ions then use water to dephosphorylate inositol</div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3488487 Sandbox Reserved 1697 2021-12-09T01:29:39Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling, the substrate of the enzyme is IP3 and the product is IP2. The amino acids of the protein hold onto the magnesium metal ions that then hold onto the water molecule, this allows for it to take off a phosphate.<br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=File:Dephosphorylation_Image.png&diff=3488476 File:Dephosphorylation Image.png 2021-12-09T01:20:01Z

<p>Abbey Morgan Pals: Shows how motif holds onto metal ions then use water to dephosphorylate inositol</p> <hr /> <div>Shows how motif holds onto metal ions then use water to dephosphorylate inositol</div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485617 Sandbox Reserved 1697 2021-12-07T04:39:46Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling. The substrate of the enzyme is IP3 and the product is IP2, <br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In this protein the amino acids do not interact with the substrate itself, instead they interact with the metal ions. When magnesium is present, and the protein therefore activated, the amino acids will hold onto the magnesium ions. These magnesium ions that interact with the inositol and water so that it can dephosphorylate the substrate. The motif of enzymes in this family is DPIDXT. In this particular protein the motif is <scene name='89/892740/Motif_view/1'>D54, E80, E79, D153, and D317</scene>. There are some mutations in the enzyme but the overall function of the protein is still the same.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485616 Sandbox Reserved 1697 2021-12-07T04:20:44Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling. The substrate of the enzyme is IP3 and the product is IP2, <br /> <br /> == Biological relevance and broader implications ==<br /> The protein 7KIR is a protype member of a family of enzymes involved in dephosphorylation IP3. The two metal ions, Magnesium and Lithium, are particularly important in activation and inhibition of inositol signaling. Since these enzymes are seen in many different organisms, with slight mutations in the motif of the enzyme without change in function, understanding the mechanics of enzyme inhibition in this metabolic pathway would allow a better understanding of metabolic pathways.<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485614 Sandbox Reserved 1697 2021-12-07T04:14:04Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, used in inositol signaling. The substrate of the enzyme is IP3 and the product is IP2, <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485613 Sandbox Reserved 1697 2021-12-07T04:10:17Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/Protein_view_2/9'>7KIR</scene> is dephosphorylating inositol, the substrate is IP2 and the product is IP. The protein studied was taken from Bos taurus but is present in many different organisms, including humans. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485612 Sandbox Reserved 1697 2021-12-07T04:07:49Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of 7KIR is dephosphorylating inositol, the substrate is IP2 and the product is IP. The protein studied was taken from Bos taurus but is present in many different organisms, including humans. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485301 Sandbox Reserved 1697 2021-12-03T17:39:57Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of <scene name='89/892740/7kir_function_scene/1'>7KIR</scene> is dephosphorylating inositol, the substrate is IP2 and the product is IP. The protein studied was taken from Bos taurus but is present in many different organisms, including humans. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485296 Sandbox Reserved 1697 2021-12-03T17:28:24Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of the protein is dephosphorylating inositol, the substrate is IP2 and the product is IP. The protein studied was taken from Bos taurus but is present in many different organisms, including humans.<br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485295 Sandbox Reserved 1697 2021-12-03T17:25:06Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of 7KIR is dephosphorylating inositol, the substrate is IP2 and the product is IP. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> <br /> == Structural highlights ==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3485292 Sandbox Reserved 1697 2021-12-03T17:13:08Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473089 Sandbox Reserved 1697 2021-11-08T01:10:52Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/8'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref><br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473088 Sandbox Reserved 1697 2021-11-08T00:59:30Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/8'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are <scene name='89/892740/Catalytic_amino_acids/1'>Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313</scene>.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions.<br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473087 Sandbox Reserved 1697 2021-11-08T00:56:26Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/8'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions.<br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473086 Sandbox Reserved 1697 2021-11-08T00:51:27Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/8'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313.<br /> <br /> == Structural highlights ==<br /> This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is 77% helix and 23% beta sheet, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions.<br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473085 Sandbox Reserved 1697 2021-11-08T00:37:38Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/8'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>.<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> The ligand of the protein is known as <scene name='89/892740/Ligand/1'>D-MYO-INOSITOL-1,4-BISPHOSPHATE</scene>, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme.<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473084 Sandbox Reserved 1697 2021-11-08T00:28:29Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/8'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>.<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473083 Sandbox Reserved 1697 2021-11-08T00:15:09Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/8'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473082 Sandbox Reserved 1697 2021-11-08T00:11:49Z

<p>Abbey Morgan Pals: </p> <hr /> <div><scene name='89/892740/Protein_view_2/6'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are gluconeogenesis and nucleotide metabolism. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3473081 Sandbox Reserved 1697 2021-11-08T00:10:43Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are gluconeogenesis and nucleotide metabolism. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3472975 Sandbox Reserved 1697 2021-11-07T06:43:48Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <<<scene name='89/892740/Protein_view_2/3'>scene name='89/892740/Protein_view_2/3'>scene name='89/892740/Protein_view_2/2'</scene</scene>>>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3472973 Sandbox Reserved 1697 2021-11-07T00:15:25Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==7KIR==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Inositol plyphosphate 1-phosphatase' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/2'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3472971 Sandbox Reserved 1697 2021-11-07T00:10:18Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='7KIR' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/2'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3472970 Sandbox Reserved 1697 2021-11-06T23:57:47Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1INP' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of of the protein are inositol phosphate (IP) signaling, other enzymes in the same family have functions that are <scene name='89/892740/Protein_view_2/2'>gluconeogenesis and nucleotide metabolism</scene>. <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3472969 Sandbox Reserved 1697 2021-11-06T23:52:41Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1INP' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> <br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3472898 Sandbox Reserved 1697 2021-11-05T14:42:22Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1INP' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> The function of the protein is to mediate <scene name='89/892740/Protein_view_2/1'>inositol phosphate (IP) signaling</scene>.<br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals https://proteopedia.org/index.php?title=Sandbox_Reserved_1697&diff=3472897 Sandbox Reserved 1697 2021-11-05T14:27:04Z

<p>Abbey Morgan Pals: </p> <hr /> <div>{{Sandbox_Reserved_BHall_F21}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1INP' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function of your protein ==<br /> <br /> == Biological relevance and broader implications ==<br /> <br /> == Important amino acids==<br /> <br /> == Structural highlights ==<br /> <br /> == Other important features ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Abbey Morgan Pals