BioLiP

Structure of PDB 1v2u Chain T

Receptor sequence

>1v2uT (length=223) Species: 9913 (Bos taurus) [Search protein sequence]

IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
ASSAIITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN

3D structure

PDB

1v2u Understanding protein-ligand interactions: the price of protein flexibility

Chain

Resolution

1.8 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	BEN	T	D189 S190 S195 V213 G219	D171 S172 S177 V191 G196	MOAD: Ki=427uM PDBbind-CN: -logKd/Ki=3.37,Ki=427uM

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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Cellular Component

PDB	RCSB:1v2u, PDBe:1v2u, PDBj:1v2u
PDBsum	1v2u
PubMed	14729347
UniProt	P00760\|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)