Structure of PDB 3cs2 Chain P

Receptor sequence
>3cs2P (length=330) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
GDRINTVRGPITISEAGFTLTHEHICASSAGFLRAWPEFFGSRKALAEKA
VRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFD
PPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELV
LKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDD
TDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALL
IKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVI
PFLREKGVPQETLAGITVTNPARFLSPTLR
3D structure
PDB3cs2 Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase.
ChainP
Resolution1.95 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 CAC P H57 W131 K169 H201 D301 H24 W98 K136 H168 D268
BS02 CO P H55 H57 K169 D301 H22 H24 K136 D268
BS03 CO P K169 H201 H230 K136 H168 H197
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:3cs2, PDBe:3cs2, PDBj:3cs2
PDBsum3cs2
PubMed18702530
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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