Structure of PDB 1v2r Chain T

Receptor sequence
>1v2rT (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
ASSRIITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1v2r Understanding protein-ligand interactions: the price of protein flexibility
ChainT
Resolution1.7 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 ANH T D189 S190 C191 Q192 S195 W215 G216 G219 C220 D171 S172 C173 Q174 S177 W193 G194 G196 C197 MOAD: Ki=278.96uM
PDBbind-CN: -logKd/Ki=3.55,Ki=278.96uM
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:1v2r, PDBe:1v2r, PDBj:1v2r
PDBsum1v2r
PubMed14729347
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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