Annotations: 2O7R

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF07859	e2o7rA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF07859	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	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	PF07859	alpha/beta hydrolase fold (Abhydrolase_3)	alpha/beta hydrolase fold	This catalytic domain is found in a very wide range of enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CXE carboxylesterase	hydrolase activity, acting on ester bonds carboxylesterase activity carboxylic ester hydrolase activity hydrolase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR002168	Lipase, GDXG, putative histidine active site	Active Site
A	IPR013094	Alpha/beta hydrolase fold-3	Domain
A	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	carboxylesterase M-CSA #407	Carboxylesterases hydrolyse carboxylic ester bonds with relatively broad substrate specificity and are useful for stereospecific synthesis and hydrolysis of esters.	Defined by 8 residues: GLY:A-92GLY:A-93SER:A-169ALA:A-170ASP:A-276MET:A-278GLN:A-282HIS:A-306 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.1.1 (PDB Primary Data) Search M-CSA Motif + EC 3.1.1.1

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 R01GM133198.