Structure of PDB 3urq Chain B

Receptor sequence
>3urqB (length=322) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
DRINTVRGPITISEAGFTLTHEHICGSSAGFLHAWPEFFGSRKALVEKAV
RGLRRARAAGVRTIVDVSTFDCGRDVSLLAEVSRAADVHIVAATGLWIDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVL
RAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDGIPWSAIASASAILGNRSWQTRALLIKALID
QGYMKQILVSNDWTFGFSSYVTNIMDVLDRVNPDGMAFIPLRVIPFLREK
GVPQETLAGITVTNPARFLSPT
3D structure
PDB3urq Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents.
ChainB
Resolution2.1 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) H21 H23 K135 H167 H196 D199 G220 D262
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 B H55 H57 K169 D301 H21 H23 K135 D262
BS02 CO B K169 H201 H230 K135 H167 H196
BS03 QMP B G60 W131 H230 D301 T303 F306 G26 W97 H196 D262 T264 F267
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:3urq, PDBe:3urq, PDBj:3urq
PDBsum3urq
PubMed22809162
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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