1NWW

Limonene-1,2-epoxide hydrolase

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	d1nwwa_	Alpha and beta proteins (a+b)	Cystatin-like	NTF2-like	Limonene-1,2-epoxide hydrolase-like	Limonene-1,2-epoxide hydrolase	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
B	d1nwwb_	Alpha and beta proteins (a+b)	Cystatin-like	NTF2-like	Limonene-1,2-epoxide hydrolase-like	Limonene-1,2-epoxide hydrolase	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Limonene-1, 2-epoxide hydrolase-like	8021283	4000596	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	NTF2-like	8033663	3000472	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	NTF2-like	8033663	3000472	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	SnoaL_1	e1nwwA1	A: a+b two layers	X: Cystatin-like	H: NTF2-like (From Topology)	T: NTF2-like	F: SnoaL_1	ECOD (1.6)
B	SnoaL_1	e1nwwB1	A: a+b two layers	X: Cystatin-like	H: NTF2-like (From Topology)	T: NTF2-like	F: SnoaL_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.450.50	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
B	3.10.450.50	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07858	Limonene-1,2-epoxide hydrolase catalytic domain (LEH)	Limonene-1,2-epoxide hydrolase catalytic domain	Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its ...	Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its structure and its novel one-step catalytic mechanism. Its main fold consists of a six-stranded mixed beta-sheet, with three N-terminal alpha helices packed to one side to create a pocket that extends into the protein core. A fourth helix lies in such a way that it acts as a rim to this pocket. Although mainly lined by hydrophobic residues, this pocket features a cluster of polar groups that lie at its deepest point and constitute the enzyme's active site [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Limonene-1,2-epoxide hydrolase	epoxide hydrolase activity ether hydrolase activity hydrolase activity, acting on ether bonds hydrolase activity limonene-1,2-epoxide hydrolase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR032710	NTF2-like domain superfamily	Homologous Superfamily
A, B	IPR013100	Limonene-1,2-epoxide hydrolase	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A	limonene-1,2-epoxide hydrolase M-CSA #644	Rhodococcus erythropolis is a species of bacteria able to grow on limonene. Its enzyme limonene epoxide hydrolase (LEH) is able to catalyse a key step in this process, namely the hydrolysis of limonene-1-2-epoxide to limonene-1-2-diol. However, the enzyme has a different fold and mechanism to the homologous family of epoxide hydrolases already known to exist, thus represents an example of convergent evolution. In fact, the enzyme bears little structural homology to any known enzyme except for kesosteriod isomerase, which catalyses a completely different reaction. The hydrolysis catalysed by LEH is enantioconvergent, therefore attracting wide interest in industrial applications.	Defined by 5 residues: TYR:A-53ASN:A-55ARG:A-99ASP:A-101ASP:A-132 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.3.2.8 (PDB Primary Data) Search M-CSA Motif + EC 3.3.2.8

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.