Structure of PDB 2zpr Chain B Binding Site BS01
Receptor Information
>2zpr Chain B (length=221) Species:
8018
(Oncorhynchus keta) [
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IVGGYECKAYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVAVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYV
QPVALPSSCAPAGTMCTVSGWGNTMSSTADGDKLQCLNIPILSYSDCNNS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFNDWLTSTMAT
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
2zpr Chain B Residue 2002 [
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Receptor-Ligand Complex Structure
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PDB
2zpr
A structural comparison of three isoforms of anionic trypsin from chum salmon (Oncorhynchus keta).
Resolution
1.75 Å
Binding residue
(original residue number in PDB)
E52 N54 V57 E59 E62
Binding residue
(residue number reindexed from 1)
E52 N54 V57 E59 E62
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
H40 D84 Q173 G174 D175 S176 G177
Catalytic site (residue number reindexed from 1)
H40 D84 Q173 G174 D175 S176 G177
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0004252
serine-type endopeptidase activity
GO:0008236
serine-type peptidase activity
GO:0046872
metal ion binding
Biological Process
GO:0006508
proteolysis
Cellular Component
GO:0005576
extracellular region
GO:0005615
extracellular space
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2zpr
,
PDBe:2zpr
,
PDBj:2zpr
PDBsum
2zpr
PubMed
19564692
UniProt
B3Y8K5
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