Structure of PDB 3urb Chain A

Receptor sequence
>3urbA (length=321) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
RINTVRGPITISEAGFTLTHEHICGSSAGFLHAWPEFFGSRKALVEKAVR
GLRRARAAGVRTIVDVSTFDCGRDVSLLAEVSRAADVHIVAATGLWIDPP
LSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLR
AAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTD
DLSYLTALAARGYLIGLDGIPWSANASASAILGNRSWQTRALLIKALIDQ
GYMKQILVSNDWTFGFSSYVTNIMDVLDRVNPDGMAFIPLRVIPFLREKG
VPQETLAGITVTNPARFLSPT
3D structure
PDB3urb Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents.
ChainA
Resolution1.77 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 G254 D301
Catalytic site (residue number reindexed from 1) H20 H22 K134 H166 H195 D198 G219 D261
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 DPF A H57 W131 K169 H201 H230 W257 D301 H22 W96 K134 H166 H195 W222 D261
BS02 CO A K169 H201 H230 K134 H166 H195
BS03 CO A H55 H57 K169 D301 H20 H22 K134 D261
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:3urb, PDBe:3urb, PDBj:3urb
PDBsum3urb
PubMed22809162
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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