Proteopedia - User contributions [en]

Sandbox GGC1

2017-05-01T14:47:59Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.

The S1 binding pocket is responsible for stabilizing the substrate before the enzyme cleaves the peptide bond. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes Phe, Tyr, and Trp. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.

The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of a monomer is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.

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

Sandbox GGC1

2017-04-30T00:50:56Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
The S1 binding pocket is responsible for stabilizing the substrate before the enzyme cleaves the peptide bond. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes Phe, Tyr, and Trp.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.

The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of a monomer is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.

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

Sandbox GGC1

2017-04-30T00:50:07Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
The S1 binding pocket is responsible for stabilizing the substrate before cleaving. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes Phe, Tyr, and Trp.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.

The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of a monomer is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.

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

Sandbox GGC1

2017-04-29T23:38:18Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
The S1 binding pocket is responsible for stabilizing the substrate before cleaving. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.

The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of a monomer is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.

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

Sandbox GGC1

2017-04-28T03:08:52Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilizing the substrate before cleaving. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.

The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of a monomer is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.

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

Sandbox GGC1

2017-04-28T03:01:31Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilizing the substrate before cleaving. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.

The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of one chain is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.

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

Sandbox GGC1

2017-04-28T02:42:20Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.

The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of one chain is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.

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

Sandbox GGC1

2017-04-28T02:26:35Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Structural Highlights and Function ==
Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
<scene name='75/752263/S1_pocket_active_site/1'>Text To Be Displayed</scene>

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

Sandbox GGC1

2017-04-28T01:56:49Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
<scene name='75/752263/S1_pocket_active_site/1'>Text To Be Displayed</scene>

== Structural highlights ==
Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold).

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

Sandbox GGC1

2017-04-28T01:49:18Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. <scene name='75/752263/S1_pocket_active_site/1'>Text To Be Displayed</scene>

== Structural highlights ==
Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold).

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

Sandbox GGC1

2017-04-28T01:46:14Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. <scene name='75/752263/S1_pocket_active_site/1'>Text To Be Displayed</scene>
== Disease ==

== Relevance ==

== Structural highlights ==
Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold).

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

Sandbox GGC1

2017-04-17T17:16:17Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. <scene name='75/752263/S1_pocket_active_site/1'>Text To Be Displayed</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-17T16:48:28Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. <scene name='75/752263/Both_active_site_and_s1/2'>Text To Be Displayed</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-17T15:28:21Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-17T15:26:26Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine alpha-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-17T15:23:33Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine alpha-chymotrypsin.<ref>PMID:15544809</ref>

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine alpha-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-17T15:23:12Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine alpha-chymotrypsin.<ref>PMID:15544809</ref>

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine alpha-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T16:50:32Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine alpha-chymotrypsin.

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine alpha-chymotrypsin is highlighted in yellow.
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T16:38:01Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine alpha-chymotrypsin.

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

== Function ==
The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue.
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine alpha-chymotrypsin is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T16:18:34Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine alpha-chymotrypsin.

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

== Function ==
The S1 binding pocket is responsible for stabilization of the substrate prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine alpha-chymotrypsin is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T16:12:50Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine alpha-chymotrypsin.

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

== Function ==
The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes P1 tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine alpha-chymotrypsin is highlighted in yellow.
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T16:10:47Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure.

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

== Function ==
The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes P1 tyrosine, tryptophan, and phenylalanine. <scene name='75/752263/Active_site/2'>The S1 pocket of the bovine alpha-chymotrypsin active Site is highlighed in yellow</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T16:02:06Z

Jackie Ha.:

Sandbox GGC1

2017-04-10T16:00:00Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold).
The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage.
This is a default text for your page '''Chymotrypsin'''. 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 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

<scene name='75/752263/Intro/1'>Chymotrypsin</scene>
== Function ==
<scene name='75/752263/Active_site/2'>Active Site is in yellow</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T15:57:44Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13, 16-146, 149-245)
The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage.
This is a default text for your page '''Chymotrypsin'''. 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 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

<scene name='75/752263/Intro/1'>Chymotrypsin</scene>
== Function ==
<scene name='75/752263/Active_site/2'>Active Site is in yellow</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3<scene name='75/752263/Three_chains/1'>Text To Be Displayed</scene>456/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/>

Sandbox GGC1

2017-04-10T15:40:45Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage.
This is a default text for your page '''Chymotrypsin'''. 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 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

<scene name='75/752263/Intro/1'>Chymotrypsin</scene>
== Function ==
<scene name='75/752263/Active_site/2'>Active Site is in yellow</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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

Sandbox GGC1

2017-04-10T15:23:58Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>
Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage.
This is a default text for your page '''Chymotrypsin'''. 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 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

<scene name='75/752263/Intro/1'>Chymotrypsin</scene>
== Function ==
<scene name='75/752263/Active_site/2'>Active Site is in yellow</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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

Sandbox GGC1

2017-04-10T15:20:12Z

Jackie Ha.:

== Chymotrypsin ==
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'>

This is a default text for your page '''Chymotrypsin'''. 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 10.1016/j.jmb.2004.09.088</ref> or to the article describing Jmol <ref>PMID:15544809</ref> to the rescue.

<scene name='75/752263/Intro/1'>Chymotrypsin</scene>
== Function ==
<scene name='75/752263/Active_site/2'>Active Site is in yellow</scene>
== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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