Structure of PDB 1v2j Chain T

Receptor sequence
>1v2jT (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
ASSRIITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1v2j Understanding protein-ligand interactions: the price of protein flexibility
ChainT
Resolution1.9 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 BEN T D189 S190 Q192 S195 V213 G219 D171 S172 Q174 S177 V191 G196 MOAD: Ki=566uM
PDBbind-CN: -logKd/Ki=3.25,Ki=566uM
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:1v2j, PDBe:1v2j, PDBj:1v2j
PDBsum1v2j
PubMed14729347
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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