Annotations: 6OWE

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ADH_zinc_N,ADH_N	e6oweA1	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_zinc_N,ADH_N	ECOD (1.6)
A	ADH_zinc_N	e6oweA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: ADH_zinc_N	ECOD (1.6)
B	ADH_zinc_N,ADH_N	e6oweB1	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_zinc_N,ADH_N	ECOD (1.6)
B	ADH_zinc_N	e6oweB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: ADH_zinc_N	ECOD (1.6)
C	ADH_zinc_N,ADH_N	e6oweC2	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_zinc_N,ADH_N	ECOD (1.6)
C	ADH_zinc_N	e6oweC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: ADH_zinc_N	ECOD (1.6)
D	ADH_zinc_N,ADH_N	e6oweD1	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_zinc_N,ADH_N	ECOD (1.6)
D	ADH_zinc_N	e6oweD2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: ADH_zinc_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.180.10	Alpha Beta	Alpha-Beta Complex	Quinone Oxidoreductase	Chain A, domain 1	CATH (utative)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
B	3.90.180.10	Alpha Beta	Alpha-Beta Complex	Quinone Oxidoreductase	Chain A, domain 1	CATH (utative)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
C	3.90.180.10	Alpha Beta	Alpha-Beta Complex	Quinone Oxidoreductase	Chain A, domain 1	CATH (utative)
C	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
D	3.90.180.10	Alpha Beta	Alpha-Beta Complex	Quinone Oxidoreductase	Chain A, domain 1	CATH (utative)
D	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00107	Zinc-binding dehydrogenase (ADH_zinc_N)	Zinc-binding dehydrogenase	-	Domain
A, B, C, D	PF08240	Alcohol dehydrogenase GroES-like domain (ADH_N)	Alcohol dehydrogenase GroES-like domain	This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure [1-2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Crotonyl-CoA carboxylase/reductase	oxidoreductase activity crotonyl-CoA reductase activity catalytic activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR013154	Alcohol dehydrogenase-like, N-terminal	Domain
A, B, C, D	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR011032	GroES-like superfamily	Homologous Superfamily
A, B, C, D	IPR013149	Alcohol dehydrogenase-like, C-terminal	Domain
A, B, C, D	IPR051603	Zinc-Containing ADH Family: Quinone Oxidoreductase/CCCR	Family
A, B, C, D	IPR010085	Crotonyl-CoA reductase	Family
A, B, C, D	IPR020843	Polyketide synthase, enoylreductase domain	Domain

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.