Structure of PDB 1o2q Chain A

Receptor sequence
>1o2qA (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1o2q Elaborate manifold of short hydrogen bond arrays mediating binding of active site-directed serine protease inhibitors.
ChainA
Resolution1.5 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 V76 E80 E52 N54 V57 V58 E62
BS02 991 A H57 D189 S190 Q192 S195 V213 S214 W215 G219 G226 V227 H40 D171 S172 Q174 S177 V191 S192 W193 G196 G204 V205 MOAD: Ki=0.021uM
PDBbind-CN: -logKd/Ki=7.68,Ki=0.021uM
BindingDB: Ki=21nM
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
GO:0097655 serpin family protein binding
Biological Process
GO:0006508 proteolysis
GO:0007586 digestion
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
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:1o2q, PDBe:1o2q, PDBj:1o2q
PDBsum1o2q
PubMed12742021
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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