Annotations: 1HT0

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ht0a1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1ht0a2	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	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1ht0b1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1ht0b2	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	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ADH_N	e1ht0A1	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	e1ht0A2	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	e1ht0B1	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	e1ht0B2	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	CLASS I ALCOHOL DEHYDROGENASE 3, GAMMA SUBUNIT	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 cellular metabolic process biological regulation carboxylic acid metabolic process primary metabolic process organic acid metabolic process hormone metabolic process retinoic acid metabolic process retinoid metabolic process cellular lipid metabolic process metabolic process cellular process diterpenoid metabolic process oxoacid metabolic process regulation of hormone levels cellular metabolic process biological regulation carboxylic acid metabolic process primary metabolic process organic acid metabolic process hormone metabolic process retinoic acid metabolic process retinoid metabolic process cellular lipid 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	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol cell periphery plasma membrane membrane membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm intracellular anatomical structure cytoplasm cellular anatomical entity cytosol cell periphery plasma membrane membrane membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013154	Alcohol dehydrogenase-like, N-terminal	Domain
A, B	IPR011032	GroES-like superfamily	Homologous Superfamily
A, B	IPR020843	Polyketide synthase, enoylreductase domain	Domain
A, B	IPR002328	Alcohol dehydrogenase, zinc-type, conserved site	Conserved Site
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR013149	Alcohol dehydrogenase-like, C-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P00326	alcohol abuse late-onset Parkinson disease alcohol dependence psoriasis Accidental poisoning by methyl alcohol carcinoma of esophagus inherited disease susceptibility lung carcinoma non-small cell lung carcinoma oropharynx cancer oral cavity cancer Parkinson disease head and neck cancer lung adenocarcinoma oral cavity neoplasm

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.