Structure of PDB 1sio Chain C Binding Site BS02
Receptor Information
>1sio Chain C (length=352) Species:
192387
(Alicyclobacillus sendaiensis) [
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TAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDEASLAQYFASLGVPA
PQVVSVSVDGASNQPTGDPSGPDGEVELDIEVAGALAPGAKFAVYFAPNT
DAGFLDAITTAIHDPTLKPSVVSISWGGPEDSWTSAAIAAMNRAFLDAAA
LGVTVLAAAGDSGSTDGEQDGLYHVDFPAASPYVLACGGTRLVASGGRIA
QETVWNDGPDGGATGGGVSRIFPLPAWQEHANVPPSANPGASSGRGVPDL
AGNADPATGYEVVIDGEATVIGGTSAVAPLFAALVARINQKLGKAVGYLN
PTLYQLPADVFHDITEGNNDIANRAQIYQAGPGWDPCTGLGSPIGVRLLQ
AL
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
1sio Chain C Residue 603 [
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Receptor-Ligand Complex Structure
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PDB
1sio
Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
D316 I317 G334 G336 D338
Binding residue
(residue number reindexed from 1)
D313 I314 G331 G333 D335
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
E78 D82 D164 S278
Catalytic site (residue number reindexed from 1)
E75 D79 D161 S275
Enzyme Commision number
?
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:1sio
,
PDBe:1sio
,
PDBj:1sio
PDBsum
1sio
PubMed
15014068
UniProt
Q8GB88
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