Annotations: 1M6H

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1m6hb1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1m6hb2	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)
A	d1m6ha1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1m6ha2	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)
B	ADH_N	e1m6hB1	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	e1m6hB2	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)
A	ADH_N	e1m6hA1	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	e1m6hA2	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)
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)
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)

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	Glutathione-dependent formaldehyde dehydrogenase	fatty acid binding organic acid binding binding ion binding anion binding lipid binding carboxylic acid binding monocarboxylic acid binding small molecule binding formaldehyde dehydrogenase (NAD+) activity oxidoreductase activity aldehyde dehydrogenase (NAD+) activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity fatty acid binding organic acid binding binding ion binding anion binding lipid binding carboxylic acid binding monocarboxylic acid binding small molecule binding formaldehyde dehydrogenase (NAD+) activity oxidoreductase activity aldehyde dehydrogenase (NAD+) activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity aldehyde dehydrogenase [NAD(P)+] activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity S-(hydroxymethyl)glutathione dehydrogenase (NADP+) 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 S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity electron transfer activity cation binding transition metal ion binding zinc ion binding metal ion binding identical protein binding protein binding	response to stimulus response to redox state multicellular organismal process system process circulatory system process regulation of blood pressure positive regulation of blood pressure biological regulation regulation of biological quality blood circulation cellular response to stimulus cellular detoxification catabolic process formaldehyde catabolic process response to stimulus response to redox state multicellular organismal process system process circulatory system process regulation of blood pressure positive regulation of blood pressure biological regulation regulation of biological quality blood circulation cellular response to stimulus cellular detoxification catabolic process formaldehyde catabolic process detoxification response to oxygen-containing compound cellular response to oxygen-containing compound aldehyde metabolic process response to toxic substance cellular detoxification of aldehyde cellular response to chemical stimulus cellular response to aldehyde response to chemical metabolic process cellular process small molecule metabolic process formaldehyde metabolic process aldehyde catabolic process small molecule catabolic process cellular response to toxic substance fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process lipid modification primary metabolic process organic acid metabolic process fatty acid omega-oxidation fatty acid oxidation lipid oxidation monocarboxylic acid metabolic process lipid metabolic process respiratory system process respiratory gaseous exchange by respiratory system response to nitrosative stress response to stress biological process involved in interspecies interaction between organisms response to lipid response to other organism response to external stimulus response to lipopolysaccharide response to biotic stimulus response to bacterium response to external biotic stimulus response to molecule of bacterial origin diterpenoid metabolic process retinoid metabolic process terpenoid metabolic process isoprenoid metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013154	Alcohol dehydrogenase-like, N-terminal	Domain
A, B	IPR002328	Alcohol dehydrogenase, zinc-type, conserved site	Conserved Site
A, B	IPR011032	GroES-like superfamily	Homologous Superfamily
A, B	IPR014183	Alcohol dehydrogenase class III	Family
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: P11766	acute myeloid leukemia ductal breast carcinoma in situ nasopharyngeal carcinoma pancreatic ductal adenocarcinoma psoriasis Alcoholic Intoxication, Chronic invasive ductal breast carcinoma osteosarcoma pancreatic intraductal papillary-mucinous carcinoma tuberculosis breast cancer lymphoplasmacytic lymphoma ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia

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.