Structure of PDB 1svn Chain A Binding Site BS02

Receptor Information
>1svn Chain A (length=269) Species: 1467 (Lederbergia lenta) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFV
PGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSG
SVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAA
SGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQ
STYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATS
LGSTNLYGSGLVNAEAATR
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 chain1svn 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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PDB1svn Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 A resolution.
Resolution1.4 Å
Binding residue
(original residue number in PDB)
A169 R170 Y171 A172 A174
Binding residue
(residue number reindexed from 1)
A163 R164 Y165 A166 A168
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D32 H64 N155 S221
Catalytic site (residue number reindexed from 1) D32 H62 N153 S215
Enzyme Commision number 3.4.21.62: subtilisin.
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:0030435 sporulation resulting in formation of a cellular spore
Cellular Component
GO:0005576 extracellular region

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Molecular Function

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Cellular Component
External links
PDB RCSB:1svn, PDBe:1svn, PDBj:1svn
PDBsum1svn
PubMed1738156
UniProtP29600|SUBS_LEDLE Subtilisin Savinase

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