1AGN

X-RAY STRUCTURE OF HUMAN SIGMA ALCOHOL DEHYDROGENASE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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)
B	d1agnb1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1agnb2	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)
D	d1agnd1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1agnd2	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	d1agna1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1agna2	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)
C	d1agnc1	All beta proteins	GroES-like	GroES-like	Alcohol dehydrogenase-like, N-terminal domain	Alcohol dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1agnc2	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	e1agnB1	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	e1agnB2	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_N	e1agnD1	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_N	ECOD (1.6)
D	ADH_zinc_N	e1agnD2	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	e1agnA1	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	e1agnA2	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_N	e1agnC1	A: beta barrels	X: GroES-like	H: GroES-related	T: Alcohol dehydrogenase-like, N-terminal domain	F: ADH_N	ECOD (1.6)
C	ADH_zinc_N	e1agnC2	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)
D	3.90.180.10	Alpha Beta	Alpha-Beta Complex	Quinone Oxidoreductase	Chain A, domain 1	CATH (4.3.0)
D	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)
C	3.90.180.10	Alpha Beta	Alpha-Beta Complex	Quinone Oxidoreductase	Chain A, domain 1	CATH (4.3.0)
C	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, 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	HUMAN SIGMA ALCOHOL DEHYDROGENASE	vitamin binding binding alcohol binding isoprenoid binding retinoid binding lipid binding retinol binding small molecule binding 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 vitamin binding binding alcohol binding isoprenoid binding retinoid binding lipid binding retinol binding small molecule binding 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 aldehyde oxidase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxidoreductase activity, acting on the aldehyde or oxo group of donors, oxygen as acceptor cation binding transition metal ion binding zinc ion binding ion binding metal ion binding anion binding ethanol binding omega-hydroxydecanoate dehydrogenase activity molecular function inhibitor activity protein binding signaling receptor binding molecular function regulator activity signaling receptor inhibitor activity receptor antagonist activity signaling receptor regulator activity	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 biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to bacterium response to external stimulus response to external biotic stimulus response to biotic stimulus fatty acid metabolic process lipid modification fatty acid omega-oxidation fatty acid oxidation lipid oxidation response to alcohol response to chemical response to oxygen-containing compound response to ethanol 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

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	IPR011032	GroES-like superfamily	Homologous Superfamily
A, B, C, D	IPR002328	Alcohol dehydrogenase, zinc-type, conserved site	Conserved Site
A, B, C, D	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR013149	Alcohol dehydrogenase-like, C-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P40394	head and neck cancer esophageal cancer larynx cancer psoriasis Alcoholic Intoxication, Chronic chronic obstructive pulmonary disease nasopharyngeal carcinoma oral cavity cancer benign laryngeal neoplasm esophageal adenocarcinoma laryngeal neoplasm neoplasm of esophagus oral cavity neoplasm pharynx cancer carcinoma of esophagus head and neck cancer esophageal cancer larynx cancer psoriasis Alcoholic Intoxication, Chronic chronic obstructive pulmonary disease nasopharyngeal carcinoma oral cavity cancer benign laryngeal neoplasm esophageal adenocarcinoma laryngeal neoplasm neoplasm of esophagus oral cavity neoplasm pharynx cancer carcinoma of esophagus non-small cell lung carcinoma 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.