4NG5

V203A horse liver alcohol dehydrogenase E complexed with NAD+ and 2,3,4,5,6-pentafluorobenzyl alcohol

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	d4ng5a1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	domestic horse,equine (Equus caballus ) [TaxId: 9796 ],	SCOPe (2.08)
A	d4ng5a2	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Alcohol dehydrogenase-like, C-terminal domain	Alcohol dehydrogenase	domestic horse,equine (Equus caballus ) [TaxId: 9796 ],	SCOPe (2.08)
B	d4ng5b1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	domestic horse,equine (Equus caballus ) [TaxId: 9796 ],	SCOPe (2.08)
B	d4ng5b2	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Alcohol dehydrogenase-like, C-terminal domain	Alcohol dehydrogenase	domestic horse,equine (Equus caballus ) [TaxId: 9796 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GroES-like	8000815	3000002	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Zinc-containing alcohol dehydrogenase-like	8000814	3000040	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zinc-containing alcohol dehydrogenase-like	8000814	3000040	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GroES-like	8000815	3000002	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	ADH_N	e4ng5A1	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_N	ECOD (1.6)
A	ADH_zinc_N	e4ng5A2	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_N	e4ng5B1	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_N	ECOD (1.6)
B	ADH_zinc_N	e4ng5B2	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 (4.3.0)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.90.180.10	Alpha Beta	Alpha-Beta Complex	Quinone Oxidoreductase	Chain A, domain 1	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00107	Zinc-binding dehydrogenase (ADH_zinc_N)	Zinc-binding dehydrogenase	-	Domain
A, B	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	Alcohol dehydrogenase E chain	alcohol dehydrogenase [NAD(P)+] activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors alcohol dehydrogenase (NAD+) activity catalytic activity all-trans-retinol dehydrogenase (NAD+) activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	diterpenoid metabolic process oxoacid metabolic process regulation of hormone levels biological regulation carboxylic acid metabolic process primary metabolic process organic acid metabolic process hormone metabolic process retinoic acid metabolic process retinoid metabolic process metabolic process cellular process small molecule metabolic process regulation of biological quality diterpenoid metabolic process oxoacid metabolic process regulation of hormone levels biological regulation carboxylic acid metabolic process primary metabolic process organic acid metabolic process hormone metabolic process retinoic acid metabolic process retinoid metabolic process metabolic process cellular process small molecule metabolic process regulation of biological quality monocarboxylic acid metabolic process terpenoid metabolic process isoprenoid metabolic process lipid metabolic process organic hydroxy compound metabolic process alcohol metabolic process olefinic compound metabolic process retinol metabolic process primary alcohol metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002328	Alcohol dehydrogenase, zinc-type, conserved site	Conserved Site
A, B	IPR013154	Alcohol dehydrogenase-like, N-terminal	Domain
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR011032	GroES-like superfamily	Homologous Superfamily
A, B	IPR013149	Alcohol dehydrogenase-like, C-terminal	Domain
A, B	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.