Structure of PDB 6fu6 Chain B

Receptor sequence
>6fu6B (length=329) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
RINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRAALVEKAVR
GLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWEDPP
LSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATNGKATPFQELVLR
AAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTD
DLSYLTALAARGYLIGLDGIPHSAIGLEDNASASALLGNRSWQTRALLIK
ALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDSVNPDGMAFIPLRVIPF
LREKGVSQETLAGITVTNPARFLSPTLRA
3D structure
PDB6fu6 Phosphotriesterase PTE_A53_4
ChainB
Resolution1.95 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) H20 H22 K134 H166 H195 D198 G219 D266
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 H20 H22 D266
BS02 ZN B H201 H230 H166 H195
BS03 TA8 B H201 H230 D301 H166 H195 D266
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:6fu6, PDBe:6fu6, PDBj:6fu6
PDBsum6fu6
PubMed
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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