3MYB

Crystal structure of enoyl-coa hydratase mycobacterium smegmatis

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3myba_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)
C	d3mybc_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)
B	d3mybb_	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Mycolicibacterium smegmatis MC2 155 ) [TaxId: 246196 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ClpP/crotonase	8059916	3000033	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ClpP/crotonase	8059916	3000033	SCOP2B (2022-06-29)
B	SCOP2 Family	Crotonase-like	8059915	4000036	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	ClpP/crotonase	8059916	3000033	SCOP2 (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	ECH_1	e3mybA1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
C	ECH_1	e3mybC1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)
B	ECH_1	e3mybB1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: ECH_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
A	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (4.3.0)
C	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
C	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (4.3.0)
B	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
B	1.10.12.10	Mainly Alpha	Orthogonal Bundle	Lyase 2-enoyl-coa Hydratase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00378	Enoyl-CoA hydratase/isomerase (ECH_1)	Enoyl-CoA hydratase/isomerase	This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Enoyl-CoA hydratase	lyase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR001753	Enoyl-CoA hydratase/isomerase	Family
A, B, C	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
A, B, C	IPR014748	Enoyl-CoA hydratase, C-terminal	Homologous Superfamily
A, B, C	IPR052377	Mitochondrial enoyl-CoA hydratase domain-containing protein	Family

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.