Structure of PDB 1v2q Chain T Binding Site BS01
Receptor Information
>1v2q Chain T (length=223) Species:
9913
(Bos taurus) [
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IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
ASSWIITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
1v2q Chain T Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
1v2q
Understanding protein-ligand interactions: the price of protein flexibility
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
E70 N72 V75 V76 E80
Binding residue
(residue number reindexed from 1)
E52 N54 V57 V58 E62
Annotation score
4
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.
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:1v2q
,
PDBe:1v2q
,
PDBj:1v2q
PDBsum
1v2q
PubMed
14729347
UniProt
P00760
|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)
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