1HDY

THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1hdya1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1hdya2	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	d1hdyb1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1hdyb2	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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GroES-like	8057524	3000002	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Zinc-containing alcohol dehydrogenase-like	8057525	3000040	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GroES-like	8057524	3000002	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zinc-containing alcohol dehydrogenase-like	8057525	3000040	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	e1hdyA1	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	e1hdyA2	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	e1hdyB1	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	e1hdyB2	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	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 cell periphery plasma membrane membrane membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm cellular anatomical structure intracellular anatomical structure cytoplasm 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: P00325	alcohol abuse esophageal squamous cell carcinoma larynx cancer esophageal cancer cerebral infarction colorectal cancer alcohol dependence obesity disorder colorectal carcinoma pancreatic intraductal papillary-mucinous carcinoma Pharyngeal Neoplasms esophageal adenocarcinoma Sjogren syndrome inherited disease susceptibility adrenal cortex carcinoma alcohol abuse esophageal squamous cell carcinoma larynx cancer esophageal cancer cerebral infarction colorectal cancer alcohol dependence obesity disorder colorectal carcinoma pancreatic intraductal papillary-mucinous carcinoma Pharyngeal Neoplasms esophageal adenocarcinoma Sjogren syndrome inherited disease susceptibility adrenal cortex carcinoma lung carcinoma myopathy breast cancer non-alcoholic fatty liver disease carcinoma of esophagus oral cavity cancer ovarian cancer pancreatic intraductal papillary-mucinous neoplasm pharynx cancer psoriasis invasive ductal breast carcinoma adenoma lung adenocarcinoma malignant colon neoplasm malignant pancreatic neoplasm atopic eczema nasopharyngeal carcinoma breast carcinoma non-small cell lung carcinoma oral cavity neoplasm pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia ductal breast carcinoma in situ pituitary cancer head and neck cancer Wernicke-Korsakoff syndrome laryngeal neoplasm adrenal cortex adenoma lung cancer benign laryngeal neoplasm neoplasm of esophagus breast fibroadenoma oropharynx cancer

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.