Structure of PDB 1s02 Chain A Binding Site BS02

Receptor Information
>1s02 Chain A (length=275) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AQSVPYGVSQIKAPALHSEGYTGSNVKVAVIDSGIDSSHPDLKVAGGASM
VPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADG
SGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVV
AAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMA
PGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSL
ENTTTKLGDSFYYGKGLINVEAAAQ
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 chain1s02 Chain A Residue 277 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1s02 Effects of engineered salt bridges on the stability of subtilisin BPN'.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G169 Y171 V174 A176 D197
Binding residue
(residue number reindexed from 1)		G169 Y171 V174 A176 D197
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D32 H64 N155 S221
Catalytic site (residue number reindexed from 1) D32 H64 N155 S221
Enzyme Commision number 3.4.21.62: subtilisin.
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1s02, PDBe:1s02, PDBj:1s02
PDBsum1s02
PubMed2127106
UniProtP00782|SUBT_BACAM Subtilisin BPN' (Gene Name=apr)

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