Structure of PDB 2vgc Chain C

Receptor sequence
>2vgcC (length=95) Species: 9913 (Bos taurus) [Search protein sequence]
TPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLV
CKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
3D structure
PDB2vgc Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) M42 G43 D44 S45 G46
Enzyme Commision number 3.4.21.1: chymotrypsin.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide C Q157 A206 W207 Q7 A56 W57
BS02 V35 C S195 S214 W215 G216 S217 S45 S64 W65 G66 S67 PDBbind-CN: -logKd/Ki=5.24,Ki=5.76uM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2vgc, PDBe:2vgc, PDBj:2vgc
PDBsum2vgc
PubMed9425066
UniProtP00766|CTRA_BOVIN Chymotrypsinogen A

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