Structure of PDB 6g1j Chain A

Receptor sequence
>6g1jA (length=331) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
GDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRAALVEKA
VRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWED
PPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATNGKATPFQELV
LRAAARASLATGVPVTTHTLASQRDGEQQAAIFESEGLSPSRVCIGHSDD
TDDLSYLTALAARGYLIGLDGIPHSAIGLEDNASASALLGNRSWQTRALL
IKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDSVNPDGMAFIPLRVI
PFLREKGVSNETLAGITVTNPARFLSPTLRA
3D structure
PDB6g1j Phosphotriesterase PTE_C23M_1
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H55 H57 K169 H201 H230 D233 G254 D301
Catalytic site (residue number reindexed from 1) H22 H24 K136 H168 H197 D200 G221 D268
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 A H55 H57 D301 H22 H24 D268
BS02 ZN A H201 H230 H168 H197
BS03 E8N A S342 T345 S309 T312
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6g1j, PDBe:6g1j, PDBj:6g1j
PDBsum6g1j
PubMed
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

[Back to BioLiP]