Structure of PDB 3cak Chain B

Receptor sequence
>3cakB (length=330) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
DRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAV
RGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVL
KAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLI
KALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIP
FLREKGVPQETLAGITVTNPARFLSPTLRA
3D structure
PDB3cak Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase.
ChainB
Resolution1.83 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 H254 D301
Catalytic site (residue number reindexed from 1) H21 H23 K135 H167 H196 D199 H220 D267
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 D267
BS02 CO B K169 H201 H230 K135 H167 H196
BS03 EFS B H57 K169 H201 D301 H23 K135 H167 D267
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:3cak, PDBe:3cak, PDBj:3cak
PDBsum3cak
PubMed18702530
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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