Structure of PDB 1k2i Chain 1

Receptor sequence
>1k2i1 (length=236) Species: 9913 (Bos taurus) [Search protein sequence]
CGVPAIQPVLIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTA
AHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITL
LKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTPDRLQQAS
LPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTL
VGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
3D structure
PDB1k2i Crystal structure of gamma-chymotrypsin in complex with 7-hydroxycoumarin.
Chain1
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) D102
Catalytic site (residue number reindexed from 1) D97
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 SN1 1 S190 C191 M192 S195 W215 G216 S217 S181 C182 M183 S186 W206 G207 S208 PDBbind-CN: -logKd/Ki=3.11,IC50=0.78mM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0097655 serpin family protein binding
Biological Process
GO:0006508 proteolysis
GO:0007586 digestion
Cellular Component
GO:0005576 extracellular region
GO:0097180 serine protease inhibitor complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1k2i, PDBe:1k2i, PDBj:1k2i
PDBsum1k2i
PubMed11846564
UniProtP00766|CTRA_BOVIN Chymotrypsinogen A

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