Structure of PDB 1v2n Chain T

Receptor sequence
>1v2nT (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSETYNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
ASSFIITSNMFCAGYLEGGKDACQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1v2n Understanding protein-ligand interactions: the price of protein flexibility
ChainT
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) G193 S195 G196
Catalytic site (residue number reindexed from 1) G175 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 T E70 N72 V75 E80 E52 N54 V57 E62
BS02 BBA T T98 Y99 D189 A190 Q192 W215 G216 G219 C220 T80 Y81 D171 A172 Q174 W193 G194 G196 C197 MOAD: Ki=1.25uM
PDBbind-CN: -logKd/Ki=5.90,Ki=1.25uM
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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Cellular Component
External links
PDB RCSB:1v2n, PDBe:1v2n, PDBj:1v2n
PDBsum1v2n
PubMed14729347
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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