Structure of PDB 1qw7 Chain A

Receptor sequence
>1qw7A (length=336) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
SIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKAL
AEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATG
LWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPF
QELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIG
HSDDTDDLSYLTALAARGYLIGLDRIPHSAIGLEDNASASALLGIRSWQT
RALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIP
LRVIPFLREKGVPQETLAGITVTNPARFLSPTLRAS
3D structure
PDB1qw7 Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CO A K169 H201 H230 R254 K140 H172 H201 R225
BS02 CO A H55 H57 K169 D301 H26 H28 K140 D272
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
PDBsum1qw7
PubMed16188223
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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