Proteopedia - User contributions [en]

Sandbox Reserved 1759

2022-12-13T05:51:23Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archaeon. The MBD enzyme is an essential intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentenyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and a significant source of intermediates for the biosynthesis of isoprenoids in archaeal organisms. Isoprenoids are the most prominent family of natural compounds, with over 80,000 chemicals. By understanding the effects of the MBD enzyme and the corresponding homologous enzymes in the MVA pathway, scientists can better understanding the evolutionary route the metabolic pathway took and its regulatory functions. Through mutagenesis of MBD, scientists were able to evaluate the catalytic importance of essential amino acids amongst homologous enzymes in other MVA pathways that emerged from divergent evolution. More research will only provide more insight into how the pathway has evolved.

== Important amino acids==

The <scene name='93/934003/Ligand/3'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128. Amino acids residue aspartate is essential for catalytic activity and protein stability. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced, the enzyme experiences a complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is primarily polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/3'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is comprised of alpha helix, parallel and anti-parallel beta-sheet, and random coils. The protein consists of two subunits with 60% alpha helixes and 40% beta-sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contain both polar and non-polar amino acids, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzyme is noted to have evolved from the ATP-dependent PMD enzyme, where it lost its ability to bind to kinase and became ATP-independent. This belief is supported by discovering that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T05:47:11Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archaeon. The MBD enzyme is an essential intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentenyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and a significant source of intermediates for the biosynthesis of isoprenoids in archaeal organisms. Isoprenoids are the most prominent family of natural compounds, with over 80,000 chemicals. By understanding the effects of the MBD enzyme and the corresponding homologous enzymes in the MVA pathway, scientists can better understanding the evolutionary route the metabolic pathway took and its regulatory functions. Through mutagenesis of MBD, scientists were able to evaluate the catalytic importance of essential amino acids amongst homologous enzymes in other MVA pathways that emerged from divergent evolution. More research will only provide more insight into how the pathway has evolved.

== Important amino acids==

The <scene name='93/934003/Ligand/3'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128. Amino acids residue aspartate is essential for catalytic activity and protein stability. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced, the enzyme experiences a complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is primarily polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/3'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T05:43:55Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archaeon. The MBD enzyme is an essential intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentenyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and a significant source of intermediates for the biosynthesis of isoprenoids in archaeal organisms. Isoprenoids are the most prominent family of natural compounds, with over 80,000 chemicals. By understanding the effects of the MBD enzyme and the corresponding homologous enzymes in the MVA pathway, scientists can better understanding the evolutionary route the metabolic pathway took and its regulatory functions. Through mutagenesis of MBD, scientists were able to evaluate the catalytic importance of essential amino acids amongst homologous enzymes in other MVA pathways that emerged from divergent evolution. More research will only provide more insight into how the pathway has evolved.

== Important amino acids==

The <scene name='93/934003/Ligand/3'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/3'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T05:37:37Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archaeon. The MBD enzyme is an essential intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentenyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and major source of intermediates for the biosynthesis of isoprenoids in archael organisms. Isoprenoids are the largest family of natural compounds, with ofer 80,000 chemicals. By understanding the effects of the MBD enzyme and the corresponding homologous enzymes in the MVA pathway, scientists can gain a better understanding of the evolutionary route the metabolic pathway took and it's regulatory functionality. Through mutagenesis of MBD, scientist were able to evaluate the catalytic importance of important amino acids amongst homologous enzymes in other MVA pathways that emerged from divergent evolution. More research will only provide more insite into how the pathway has evolved.

== Important amino acids==

The <scene name='93/934003/Ligand/3'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/3'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T05:33:25Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archeaon. The MBD enzyme is an important intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and major source of intermediates for the biosynthesis of isoprenoids in archael organisms. Isoprenoids are the largest family of natural compounds, with ofer 80,000 chemicals. By understanding the effects of the MBD enzyme and the corresponding homologous enzymes in the MVA pathway, scientists can gain a better understanding of the evolutionary route the metabolic pathway took and it's regulatory functionality. Through mutagenesis of MBD, scientist were able to evaluate the catalytic importance of important amino acids amongst homologous enzymes in other MVA pathways that emerged from divergent evolution. More research will only provide more insite into how the pathway has evolved.

== Important amino acids==

The <scene name='93/934003/Ligand/3'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/3'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T05:27:43Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archeaon. The MBD enzyme is an important intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and major source of intermediates for the biosynthesis of isoprenoids in archael organisms. Isoprenoids are the largest family of natural compounds, with ofer 80,000 chemicals. By understanding the effects of the MBD enzyme and the corresponding homologous enzymes in the MVA pathway, scientists can gain a better understanding of the evolutionary route the metabolic pathway took and it's regulatory functionality. Through mutagenesis of MBD, scientist were able to evaluate the catalytic importance of important amino acids amongst homologous enzymes in other MVA pathways that emerged from divergent evolution. More research will only provide more insite into how the pathway has evolved.

== Important amino acids==

The <scene name='93/934003/Ligand/2'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T05:07:49Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archeaon. The MBD enzyme is an important intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and major source of intermediates for the biosynthesis of isoprenoids in archael organisms. Isoprenoids are the largest family of natural compounds, with ofer 80,000 chemicals. By understanding the effects of the MBD enzyme and the corresponding homologous enzymes in the MVA pathway, scientists can gain a better understanding of the evolutionary route the metabolic pathway took and it's regulatory functionality. Through mutagenesis of MBD, scientist were able to evaluate the catalytic importance of important amino acids amongst homologous enzymes in other MVA pathways that emerged from divergent evolution. More research will only provide more insite into how the pathway has evolved.

== Important amino acids==

The <scene name='93/934003/Ligand/2'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/2'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/2'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T04:39:49Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene> from ''Picrophilus torrid'', a thermoacidophilic archeaon. The MBD enzyme is an important intermediate of the mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

The MVA pathway is an essential metabolic pathway and major source of intermediates for the biosynthesis of isoprenoids in Thermoplasma-type organisms. By understanding the effects of the MBD enzyme, scientists are provided
IP
Understanding the components of the mevalonate pathway

== Important amino acids==

The <scene name='93/934003/Ligand/2'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/2'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/2'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T04:21:33Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type mevalonate (MVA) pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

IP
Understanding the components of the mevalonate pathway

== Important amino acids==

The <scene name='93/934003/Ligand/2'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/2'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/2'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T04:07:46Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

IP
Understanding the components of the mevalonate pathway

== Important amino acids==

The <scene name='93/934003/Ligand/2'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/2'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/2'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T03:52:34Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Ligand/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/2'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/2'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T03:46:30Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Ligand/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/1'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/1'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T03:21:48Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Ligand/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/1'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When Asp281 is replaced the enzyme experiences lose in decarboxylase function. When <scene name='93/934003/Asp309/1'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T03:18:06Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/1'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When Asp281 is replaced the enzyme experiences lose in decarboxylase function. When <scene name='93/934003/Asp309/1'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T03:11:39Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When Asp281 is replaced the enzyme experiences lose in decarboxylase function. When <scene name='93/934003/Asp309/1'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T02:49:21Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When Asp281 is replaced the enzyme experiences lose in decarboxylase function. When Asp309 is replaced the enzyme experiences complete loss of MBD activity.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T02:48:19Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme <scene name='93/934003/Protein_of_interest/1'>mevalonate 3,5-bisphosphate decarboxylase (MBD)</scene>. The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When Asp281 is replaced the enzyme experiences lose in decarboxylase function. When Asp309 is replaced the enzyme experiences complete loss of MBD activity.

== Structural highlights ==
The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

.In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-13T02:35:13Z

Katherine Hull:

Sandbox Reserved 1759

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Katherine Hull:

Sandbox Reserved 1759

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Katherine Hull:

Sandbox Reserved 1759

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Katherine Hull:

Sandbox Reserved 1759

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Katherine Hull:

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Katherine Hull:

Sandbox Reserved 1759

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Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>.

== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and random coils. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-12T00:52:06Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>.

== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-12T00:49:25Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well.

== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-12T00:37:45Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand, which is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-12T00:16:46Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. Each subunit contains 9 alpha helix and 15 beta sheets. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>.

The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein and

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-11T23:49:54Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. Each subunit contains 9 alpha helix and 15 beta sheets. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a 3D globular protein.

The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein and

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-11T23:43:09Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. Each subunit contains 9 alpha helix and 15 beta sheets. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a 3D globular protein.

<scene name='93/934003/Space_filling/1'>Space filling</scene>

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T23:10:15Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The <scene name='93/934003/60_alpha_and_40_beta/1'>protein</scene> consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the structure. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

<scene name='93/934003/Space_filling/1'>Space filling</scene>

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T23:07:29Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha and 40% beta breakdown when viewing the<scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

<scene name='93/934003/Space_filling/1'>Space filling</scene>

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T23:06:34Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha and 40% beta breakdown in a <scene name='93/934003/60_alpha_and_40_beta/1'>cartoon view</scene>. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

<scene name='93/934003/Space_filling/1'>Space filling</scene>

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T23:04:33Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. When the alpha and beta structures are The protein consists of two major domains with what appears to be a 60% alpha and 40% beta in a <scene name='93/934003/60_alpha_and_40_beta/1'>cartoon view</scene>. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

40 beta 60 alpha

<scene name='93/934003/Space_filling/1'>Space filling</scene>

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T22:37:40Z

Katherine Hull:

==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

<scene name='93/934003/Space_filling/1'>Space filling</scene>

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T22:16:15Z

Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T22:12:31Z

Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase. The MVA3,5-bisphosphate decarboxylase enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MVA3,5-bisphosphate decarboxylase is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MVA 3,5-bisphosphate decarboxylase acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T22:10:29Z

Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase. The MVA3,5-bisphosphate decarboxylase enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The basic function of MVA3,5-bisphosphate decarboxylase is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MVA 3,5-bisphosphate decarboxylase acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

</StructureSection>
== References ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T22:09:46Z

Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''>

== Function of your protein ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase. The MVA3,5-bisphosphate decarboxylase enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The basic function of MVA3,5-bisphosphate decarboxylase is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MVA 3,5-bisphosphate decarboxylase acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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 ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T22:04:29Z

Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase. The MVA3,5-bisphosphate decarboxylase enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The basic function of MVA3,5-bisphosphate decarboxylase is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MVA 3,5-bisphosphate decarboxylase acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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 ==
<ref>PMID:24755225</ref>

<references/>

Sandbox Reserved 1759

2022-12-09T21:51:49Z

Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase. The MVA3,5-bisphosphate decarboxylase enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The basic function of MVA3,5-bisphosphate decarboxylase is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MVA 3,5-bisphosphate decarboxylase acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction.

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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 ==
<ref> 24755225 </ref>

<references/>

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{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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 ==
<ref> 24755225 </ref>

<references/>

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Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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 ==
<ref> 24755225 </ref>

<ref> 24755225 </ref>

<references/>

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Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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 ==

<ref> 24755225 </ref>

<references/>

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Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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 ==
<ref>24755225</ref>
<references/>

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Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet.

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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Katherine Hull:

{{{Sandbox_Reserved_BHall_F22}}
==Mevalonate 3,5-Bisphosphate Decarboxylase Structure==
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' 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 ==

<scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>)
== Biological relevance and broader implications ==

== Important amino acids==

Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128.
== Structural highlights ==
The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, The amino acid Arg148 that h-bonds to the OLA ligand is contained within a beta sheet.

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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Katherine Hull:

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Katherine Hull:

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Katherine Hull: