2OR0

Structural Genomics, the crystal structure of a putative hydroxylase from Rhodococcus sp. RHA1

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e2or0A1	A: beta complex topology	X: Acyl-CoA dehydrogenase middle domain-like (From Topology)	H: Acyl-CoA dehydrogenase middle domain-like (From Topology)	T: Acyl-CoA dehydrogenase middle domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
A	F_UNCLASSIFIED	e2or0A2	A: alpha arrays	X: Acyl-CoA dehydrogenase N-terminal domain-like (From Topology)	H: Acyl-CoA dehydrogenase N-terminal domain-like (From Topology)	T: Acyl-CoA dehydrogenase N-terminal domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF08028	e2or0A3	A: alpha bundles	X: Bromodomain-like	H: Acyl-CoA dehydrogenase C-terminal domain-like (From Topology)	T: Acyl-CoA dehydrogenase C-terminal domain-like	F: PF08028	ECOD (1.6)
B	F_UNCLASSIFIED	e2or0B2	A: beta complex topology	X: Acyl-CoA dehydrogenase middle domain-like (From Topology)	H: Acyl-CoA dehydrogenase middle domain-like (From Topology)	T: Acyl-CoA dehydrogenase middle domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	F_UNCLASSIFIED	e2or0B3	A: alpha arrays	X: Acyl-CoA dehydrogenase N-terminal domain-like (From Topology)	H: Acyl-CoA dehydrogenase N-terminal domain-like (From Topology)	T: Acyl-CoA dehydrogenase N-terminal domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF08028	e2or0B1	A: alpha bundles	X: Bromodomain-like	H: Acyl-CoA dehydrogenase C-terminal domain-like (From Topology)	T: Acyl-CoA dehydrogenase C-terminal domain-like	F: PF08028	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.540.10	Mainly Alpha	Orthogonal Bundle	Butyryl-Coa Dehydrogenase, subunit A	domain 1	CATH (4.3.0)
A	2.40.110.10	Mainly Beta	Beta Barrel	Butyryl-CoA Dehydrogenase, subunit A	domain 2	CATH (4.3.0)
A	1.20.140.10	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)
B	1.10.540.10	Mainly Alpha	Orthogonal Bundle	Butyryl-Coa Dehydrogenase, subunit A	domain 1	CATH (4.3.0)
B	2.40.110.10	Mainly Beta	Beta Barrel	Butyryl-CoA Dehydrogenase, subunit A	domain 2	CATH (4.3.0)
B	1.20.140.10	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF08028	Acyl-CoA dehydrogenase, C-terminal domain (Acyl-CoA_dh_2)	Acyl-CoA dehydrogenase, C-terminal domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Hydroxylase	oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors catalytic activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013107	Acyl-CoA dehydrogenase, C-terminal domain	Domain
A, B	IPR009100	Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily	Homologous Superfamily
A, B	IPR046373	Acyl-CoA oxidase/dehydrogenase, middle domain superfamily	Homologous Superfamily
A, B	IPR036250	Acyl-CoA dehydrogenase-like, C-terminal	Homologous Superfamily
A, B	IPR037069	Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily	Homologous Superfamily

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.