Structure of PDB 2o4m Chain P

Receptor sequence
>2o4mP (length=331) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
GDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKA
VRGLRRARAAGVRTIVDVSTFDGGRDVSLLAEVSRAADVHIVAATGLWGD
PPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELV
LKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDD
TDDLSYLTALAARGYLIGLDHIPYSAIGLEDNASASALLGIRSWQTRALL
IKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVI
PFLREKGVPQETLAGITVTNPARFLSPTLRA
3D structure
PDB2o4m Structure of Phosphotriesterase mutant I106G/F132G/H257Y
ChainP
Resolution1.64 Å
3D
structure
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Enzymatic activity
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 ZN P H55 H57 K169 D301 H22 H24 K136 D268
BS02 ZN P K169 H201 H230 K136 H168 H197
BS03 ZN P D233 H254 D200 H221
BS04 ZN P E48 H123 E15 H90
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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Cellular Component
External links
PDB RCSB:2o4m, PDBe:2o4m, PDBj:2o4m
PDBsum2o4m
PubMed
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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