Structure of PDB 4gy0 Chain B

Receptor sequence
>4gy0B (length=326) Species: 32630 (synthetic construct) [Search protein sequence]
RINTVRGPITISEVGFTLTHEHICGSSAGFLRAWPEFFGSREALVEKAVR
GLRRARAAGVRTIVDVSTFDLGRDVRLLAEVSRAADVHIVAATGVWLDPP
LSIRMRSVEELTQFFLREIQYGIEDTGIRAGIIKVAITGKVTPFQELVLR
AAARASLATGVPVITHTAGSQRGGEQQAAIFESEGLSPSRVCIGHSDETD
DLSYLTALAARGYLIGLDRIPHSAIGLEDNASATAFMGSRSWQTRALLIK
ALIDQGYMKQILVSNDWLFGISSYVTNFMDVMDSVNPDGMAFIPLRVIPF
LREKGIPQETLAGITVTNPARFLSPT
3D structure
PDB4gy0 Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme
ChainB
Resolution1.85 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 E233 R254 D301
Catalytic site (residue number reindexed from 1) H20 H22 K134 H166 H195 E198 R219 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 ZN B H55 H230 H20 H195
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:4gy0, PDBe:4gy0, PDBj:4gy0
PDBsum4gy0
PubMed23212386
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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