Annotations: 1ZOI

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d1zoic_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Haloperoxidase	automated matches	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
A	d1zoia_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Haloperoxidase	automated matches	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
B	d1zoib_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Haloperoxidase	automated matches	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	alpha/beta-Hydrolases	8064146	3000102	SCOP2B (2022-06-29)
A	SCOP2 Family	Haloperoxidase	8064145	4000717	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	alpha/beta-Hydrolases	8064146	3000102	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8064146	3000102	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)
C	Hydrolase_4_1	e1zoiC1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_1	ECOD (1.6)
A	Hydrolase_4_1	e1zoiA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_1	ECOD (1.6)
B	Hydrolase_4_1	e1zoiB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00561	alpha/beta hydrolase fold (Abhydrolase_1)	alpha/beta hydrolase fold	This catalytic domain is found in a very wide range of enzymes.	Domain

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR000073	Alpha/beta hydrolase fold-1	Domain
A, B, C	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	esterase M-CSA #733	Esterase (EST), isolated from Pseudomonas putida, catalyses the hydrolysis of methyl esters. Of particular interest is the stereoselective hydrolysis of DL-beta-acetylthioisobutyrate acid (DL-MATI) to D-beta-acetylthioisobutyric acid (DAT). This is because DAT is an important intermediate in the synthesis of the medicinally important angiotensin-converting enzyme inhibitors. The mechanism of action of EST is similar to the serine protease mechanism.	Defined by 6 residues: TRP:A-31SER:A-97THR:A-98ALA:A-122ASP:A-227HIS:A-256 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1 (PDB Primary Data) Search M-CSA Motif + EC 3.1

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.