Structure of PDB 2zpr Chain B Binding Site BS01

Receptor Information
>2zpr Chain B (length=221) Species: 8018 (Oncorhynchus keta) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGYECKAYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVAVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYV
QPVALPSSCAPAGTMCTVSGWGNTMSSTADGDKLQCLNIPILSYSDCNNS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFNDWLTSTMAT
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2zpr Chain B Residue 2002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2zpr A structural comparison of three isoforms of anionic trypsin from chum salmon (Oncorhynchus keta).
Resolution1.75 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 score4
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
PDBsum2zpr
PubMed19564692
UniProtB3Y8K5

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