Structure of PDB 1c9p Chain A

Receptor sequence
>1c9pA (length=223) Species: 9823 (Sus scrofa) [Search protein sequence]
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL
GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLDSRV
ATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKS
SYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQK
NKPGVYTKVCNYVNWIQQTIAAN
3D structure
PDB1c9p Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmin system.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H40 D84 Q174 G175 D176 S177 G178
Enzyme Commision number 3.4.21.4: trypsin.
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 CA A E70 N72 V75 E80 E52 N54 V57 E62
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007586 digestion
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Cellular Component
External links
PDB RCSB:1c9p, PDBe:1c9p, PDBj:1c9p
PDBsum1c9p
PubMed10512718
UniProtP00761|TRYP_PIG Trypsin

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