Structure of PDB 1bzx Chain E Binding Site BS01
Receptor Information
>1bzx Chain E (length=222) Species:
8030
(Salmo salar) [
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IVGGYECKPYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVEVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYV
QPVALPTSCAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFNDWLTSTMASY
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
1bzx Chain E Residue 700 [
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Receptor-Ligand Complex Structure
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PDB
1bzx
The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
E70 N72 V75 E77 E80
Binding residue
(residue number reindexed from 1)
E52 N54 V57 E59 E62
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
D102 G193 S195 G196
Catalytic site (residue number reindexed from 1)
D84 G174 S176 G177
Enzyme Commision number
3.4.21.4
: trypsin.
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
GO:0007586
digestion
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:1bzx
,
PDBe:1bzx
,
PDBj:1bzx
PDBsum
1bzx
PubMed
9760170
UniProt
P35031
|TRY1_SALSA Trypsin-1
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