Navigation Tabs
HIGH RESOLUTION STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA External Resource: Annotation Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) B SCOP2B Superfamily Metallo-dependent hydrolases 8033495 3000428 SCOP2B (2022-06-29) A SCOP2B Superfamily Metallo-dependent hydrolases 8033495 3000428 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) B PTE e1hzyB1 A: a/b barrels X: TIM beta/alpha-barrel H: TIM barrels (From Topology) T: TIM barrels F: PTE ECOD (1.6) A PTE e1hzyA1 A: a/b barrels X: TIM beta/alpha-barrel H: TIM barrels (From Topology) T: TIM barrels F: PTE ECOD (1.6)
Chains Polymer Molecular Function Biological Process Cellular Component PHOSPHOTRIESTERASE
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage Chains Enzyme Name Description Catalytic Residues aryldialkylphosphatase
M-CSA #159 Phosphotriesterase (PTE) contains a binuclear zinc catalytic site, a structural motif characteristic of the amidohydrolase superfamily. The enzyme acts to hydrolyse phosphoesters via nucleophilic attack at the substrate PO bond from the bridging hydroxide ligand.
 View MoreDefined by 8 residues: HIS:A-22 [auth A-55] HIS:A-24 [auth A-57] LYS:A-136 [auth A-169] HIS:A-168 [auth A-201] HIS:A-197 [auth A-230] ASP:A-200 [auth A-233] HIS:A-221 [auth A-254] ASP:A-268 [auth A-301]
|
Explore in 3D :
M-CSA Motif Definition