Structure of PDB 1dlk Chain D

Receptor sequence
>1dlkD (length=230) Species: 9913 (Bos taurus) [Search protein sequence]
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDV
VVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFS
QTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSN
TNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSW
GSSTCSTSTPGVYARVTALVNWVQQTLAAN
3D structure
PDB1dlk Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.
ChainD
Resolution2.14 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 M192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H42 D87 M177 G178 D179 S180 G181
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 D E20 S26 W27 P28 A120 C122 Q157 S159 W207 E5 S11 W12 P13 A105 C107 Q142 S144 W192
BS02 peptide D H57 L97 T98 K175 S190 M192 S195 S214 W215 G216 S217 H42 L82 T83 K160 S175 M177 S180 S199 W200 G201 S202
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:1dlk, PDBe:1dlk, PDBj:1dlk
PDBsum1dlk
PubMed10713514
UniProtP00766|CTRA_BOVIN Chymotrypsinogen A

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