Structure of PDB 6aml Chain G

Receptor sequence
>6amlG (length=315) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
GDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKA
VRGLRRASAAGVRTIVDVSTFDLGRDVSLLAEVSRAADVHIVAATGLWLD
PPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKVTPFQELV
LRAAARASLATGVPVTTHTAASQRGGEQQAAILESEGLSPSRVCIGHSDA
ADDLSYHTALAARGYLIGLDSIPHSAVRSWQTRALLIKALIDQGYTKQIL
VSNDWLFGISSYVTNIMDVMDSGNPDGMAFIPLRVIPFLREKGIPQETLA
GITVTNPARFLSPTL
3D structure
PDB6aml Phosphotriesterase variant S8
ChainG
Resolution1.46 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 A233 S254 D301
Catalytic site (residue number reindexed from 1) H22 H24 K136 H168 H197 A200 S221 D254
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 G H55 H57 K169 D301 H22 H24 K136 D254
BS02 ZN G 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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Biological Process
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Cellular Component
External links
PDB RCSB:6aml, PDBe:6aml, PDBj:6aml
PDBsum6aml
PubMed
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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