Structure of PDB 6fqe Chain B

Receptor sequence
>6fqeB (length=340) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
ISEFITNSGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGS
RAALVEKAVRGLRRARAAGVRTIVDVSTFDAGRDVSLLAEVSRAADVHIV
AATGLWEDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATQGK
ATPFQELVLRAAARASLATGVPVTTHTFASQRDGEQQAAIFESEGLSPSR
VCIGHSDDTDDLSYLTALAARGYLIGLDGIPHSAIGLEDNASASALLGNR
SWQTRALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDSVNPDGM
AFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPTLRAS
3D structure
PDB6fqe Phosphotriesterase PTE_A53_4
ChainB
Resolution1.75 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) H30 H32 K144 H176 H205 D208 G229 D276
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 B H55 H57 D301 H30 H32 D276
BS02 ZN B H201 H230 H176 H205
BS03 D6K B H57 W131 D301 F306 H32 W106 D276 F281
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:6fqe, PDBe:6fqe, PDBj:6fqe
PDBsum6fqe
PubMed
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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