1HZY

HIGH RESOLUTION STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE FROM PSEUDOMONAS DIMINUTA

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1hzya_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	Phosphotriesterase-like	Phosphotriesterase (parathion hydrolase, PTE)	(Brevundimonas diminuta ) [TaxId: 293 ],	SCOPe (2.08)
B	d1hzyb_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	Phosphotriesterase-like	Phosphotriesterase (parathion hydrolase, PTE)	(Brevundimonas diminuta ) [TaxId: 293 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Metallo-dependent hydrolases	8033495	3000428	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Metallo-dependent hydrolases	8033495	3000428	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
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)
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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
B	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02126	Phosphotriesterase family (PTE)	Phosphotriesterase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PHOSPHOTRIESTERASE	cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding phosphoric ester hydrolase activity aryldialkylphosphatase activity hydrolase activity, acting on ester bonds phosphoric triester hydrolase activity hydrolase activity catalytic activity	catabolic process metabolic process	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR017947	Aryldialkylphosphatase, zinc-binding site	Binding Site
A, B	IPR001559	Phosphotriesterase	Family
A, B	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A, B	IPR032466	Metal-dependent hydrolase	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	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.	Defined 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 Search M-CSA Motif EC: 3.1.8.1 (PDB Primary Data) Search M-CSA Motif + EC 3.1.8.1

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.