Proteopedia - User contributions [en]

Sandbox Reserved 1756

2022-12-13T16:30:38Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

Each C=O consists of two oxygen atoms that form hydrogen bonds, which stabilize the secondary structure. A polar amino acid residue is on the outside and a nonpolar amino acid is inside the alpha helix since non-polar amino acids do not react with water. Beta sheet runs in an antiparallel direction of non-polar and polar amino acids.

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site.

== Other important features ==

<scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding.

<scene name='93/934000/Aa_polar/1'>
Polar amino acids</scene> is important part of protein structure. It is found usually on the outside of the alpha and beta that is because of its water-loving quality. It help to determine the 3-D structure and its specifically function.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T16:30:16Z

Sumitra Basnet:

Sandbox Reserved 1756

2022-12-13T16:28:55Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

he pink helix represents the alpha helix, and the yellow sheet represents
the beta sheet. Each C=O consists of two oxygen atoms that form
hydrogen bonds, which stabilize the secondary structure. A polar amino
acid residue is on the outside and a nonpolar amino acid is inside the alpha
helix since non-polar amino acids do not react with water. Beta sheet runs
in an antiparallel direction of non-polar and polar amino acids.

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

== Other important features ==

<scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding.

<scene name='93/934000/Aa_polar/1'>
Polar amino acids</scene> is important part of protein structure. It is found usually on the outside of the alpha and beta that is because of its water-loving quality. It help to determine the 3-D structure and its specifically function.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T16:28:01Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

== Other important features ==

<scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding.

<scene name='93/934000/Aa_interactions/1'>Hydrophobic interaction</scene> is important

<scene name='93/934000/Aa_polar/1'>
Polar amino acids</scene> is important part of protein structure. It is found usually on the outside of the alpha and beta that is because of its water-loving quality. It help to determine the 3-D structure and its specifically function.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T16:16:34Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

== Other important features ==

<scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding.

<scene name='93/934000/Aa_interactions/1'>Hydrophobic interaction</scene> is important

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T09:47:50Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

== Other important features ==

<scene name='93/934000/Ball_and_stick_model/1'>
ball and stick model</scene> to help understand on how molecules are bond to each other.

<scene name='93/934000/Aa_interactions/1'>Hydrophobic interaction</scene> is important

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T09:31:05Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

The beta sheet contains 1 of the 3 catalytic amino acids.

== Other important features ==

<scene name='93/934000/Ball_and_stick_model/1'>
ball and stick model</scene> to help understand on how molecules are bond to each other.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T09:23:46Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

The beta sheet contains 1 of the 3 catalytic amino acids.

== Other important features ==

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T09:22:54Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

The beta sheet contains 1 of the 3 catalytic amino acids.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T09:13:17Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}

Ornithine Aminotransferase

<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of two substrates, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

The beta sheet contains 1 of the 3 catalytic amino acids.

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1756

2022-12-13T09:08:55Z

Sumitra Basnet:

{{Sandbox_Reserved_BHall_F22}}
Ornithine Aminotransferase
<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of two substrates, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site

The beta sheet contains 1 of the 3 catalytic amino acids.

</StructureSection>
== References ==
<references/>

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Ornithine Aminotransferase
<StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene>

== Function of your protein ==

The specific function of ornithine aminotransferase is responsible for converting ornithine into pyrroline-5-carboxylate (P5C) to another molecule. Glutamate and proline are the amino acids that can be produced from P5C

Homo sapiens is the organism from which the HOAT is derived

These enzymes are comprised of two substrates, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292.

== Biological relevance and broader implications ==

A type of cancer that is being studied is hepatocellular carcinoma, an aggressive form of liver cancer. Scientists have determined that HOAT is over-expressed in specific cells.

The study of the HOAT enzyme has enabled scientists to gain a more thorough understanding of metabolism. This is because it provides information about how the human body responds to specific stimuli through the use of this enzyme.

== Important amino acids==
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>.
<scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene>

Hydrogen bonding - Val 143, Asp 263, Gly 142

Covalent bonding - Lys 292

Salt bridge - Asp 263 and Arg

Pi-stacking - Phe 177

== Structural highlights ==

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.

Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein

<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>

The beta sheet contains 1 of the 3 catalytic amino acids.

</StructureSection>
== References ==
<references/>

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Ornithine Aminotransferase =
<StructureSection load='7T9Z' size='340' side='right' caption='OAT Protein' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.

== Function of your protein ==

== Biological relevance and broader implications ==

== Important amino acids==

== Structural highlights ==

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.

</StructureSection>
== References ==
<references/>

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{{Sandbox_Reserved_BHall_F22}}
==Ornithine Aminotransferase =
<StructureSection load='7T9Z' size='340' side='right' caption='OAT Protein' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.

== Function of your protein ==

== Biological relevance and broader implications ==

== Important amino acids==

== Structural highlights ==

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.

</StructureSection>
== References ==
<references/>

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Sumitra Basnet: New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='7T9Z' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''"sandbox1756"'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

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.

</StructureSection>
== References ==
<references/>