Structure of PDB 3vgc Chain C

Receptor sequence
>3vgcC (length=95) Species: 9913 (Bos taurus) [Search protein sequence]
TPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLV
CKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
3D structure
PDB3vgc Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.
ChainC
Resolution1.67 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 SRB C S190 M192 S195 V213 S214 W215 G216 S217 S40 M42 S45 V63 S64 W65 G66 S67 PDBbind-CN: -logKd/Ki=5.51,Ki=3.11uM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3vgc, PDBe:3vgc, PDBj:3vgc
PDBsum3vgc
PubMed9425066
UniProtP00766|CTRA_BOVIN Chymotrypsinogen A

[Back to BioLiP]