Structure of PDB 1svn Chain A Binding Site BS02
Receptor Information
>1svn Chain A (length=269) Species:
1467
(Lederbergia lenta) [
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AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFV
PGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSG
SVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAA
SGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQ
STYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATS
LGSTNLYGSGLVNAEAATR
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
1svn Chain A Residue 277 [
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Receptor-Ligand Complex Structure
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PDB
1svn
Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 A resolution.
Resolution
1.4 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 score
4
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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Biological Process
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Cellular Component
External links
PDB
RCSB:1svn
,
PDBe:1svn
,
PDBj:1svn
PDBsum
1svn
PubMed
1738156
UniProt
P29600
|SUBS_LEDLE Subtilisin Savinase
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