Structure of PDB 1qw7 Chain B Binding Site BS01
Receptor Information
>1qw7 Chain B (length=336) Species:
293
(Brevundimonas diminuta) [
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SIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKAL
AEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATG
LWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPF
QELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIG
HSDDTDDLSYLTALAARGYLIGLDRIPHSAIGLEDNASASALLGIRSWQT
RALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIP
LRVIPFLREKGVPQETLAGITVTNPARFLSPTLRAS
Ligand information
Ligand ID
CO
InChI
InChI=1S/Co/q+2
InChIKey
XLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341
[Co++]
Formula
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
1qw7 Chain B Residue 603 [
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Receptor-Ligand Complex Structure
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PDB
1qw7
Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
H55 H57 K169 D301
Binding residue
(residue number reindexed from 1)
H26 H28 K140 D272
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H55 H57 K169 H201 H230 D233 R254 D301
Catalytic site (residue number reindexed from 1)
H26 H28 K140 H172 H201 D204 R225 D272
Enzyme Commision number
3.1.8.1
: aryldialkylphosphatase.
Gene Ontology
Molecular Function
GO:0004063
aryldialkylphosphatase activity
GO:0008270
zinc ion binding
GO:0016787
hydrolase activity
GO:0016788
hydrolase activity, acting on ester bonds
GO:0046872
metal ion binding
Biological Process
GO:0009056
catabolic process
Cellular Component
GO:0005886
plasma membrane
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1qw7
,
PDBe:1qw7
,
PDBj:1qw7
PDBsum
1qw7
PubMed
16188223
UniProt
P0A434
|OPD_BREDI Parathion hydrolase (Gene Name=opd)
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