Structure of PDB 1cnm Chain A Binding Site BS02
Receptor Information
>1cnm Chain A (length=279) Species:
37998
(Parengyodontium album) [
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AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFE
GRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNG
SGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQS
SGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLD
IFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACR
YIADTANKGDLSNIPFGTVNLLAYNNYQA
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
1cnm Chain A Residue 281 [
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Receptor-Ligand Complex Structure
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PDB
1cnm
Enhancement of catalytic efficiency of enzymes through exposure to anhydrous organic solvent at 70 degrees C. Three-dimensional structure of a treated serine proteinase at 2.2 A resolution.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
T16 D260
Binding residue
(residue number reindexed from 1)
T16 D260
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
D39 H69 N161 S224
Catalytic site (residue number reindexed from 1)
D39 H69 N161 S224
Enzyme Commision number
3.4.21.64
: peptidase K.
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:1cnm
,
PDBe:1cnm
,
PDBj:1cnm
PDBsum
1cnm
PubMed
10737944
UniProt
P06873
|PRTK_PARAQ Proteinase K (Gene Name=PROK)
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