Structure of PDB 1jgm Chain A

Receptor sequence
>1jgmA (length=333) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
TGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEK
AVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWF
DPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQEL
VLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSD
DTDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRAL
LIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRV
IPFLREKGVPQETLAGITVTNPARFLSPTLRAS
3D structure
PDB1jgm High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta.
ChainA
Resolution1.3 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) H23 H25 K137 H169 H198 D201 H222 D269
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 CD A H55 H57 K169 D301 H23 H25 K137 D269
BS02 CD A K169 H201 H230 K137 H169 H198
BS03 PEL A M293 G348 N353 M261 G316 N321
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:1jgm, PDBe:1jgm, PDBj:1jgm
PDBsum1jgm
PubMed11258882
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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