2ONO

Arg475Gln Mutant of Mitochondrial Aldehyde Dehydrogenase, apo form, pseudo-merohedrally twinned

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	d2onoa_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2onoc_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2onod_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d2onoe_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d2onof_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d2onog_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d2onoh_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2onob_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	ALDH-like	Aldehyde reductase (dehydrogenase), ALDH	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	ALDH-like	8033787	3001479	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ALDH-like	8033787	3001479	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ALDH-like	8033787	3001479	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	ALDH-like	8033787	3001479	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	ALDH-like	8033787	3001479	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	ALDH-like	8033787	3001479	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	ALDH-like	8033787	3001479	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ALDH-like	8033787	3001479	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	Aldedh_2nd	e2onoA1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
A	Aldedh_1st_1	e2onoA2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
C	Aldedh_2nd	e2onoC1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
C	Aldedh_1st_1	e2onoC2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
D	Aldedh_2nd	e2onoD2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
D	Aldedh_1st_1	e2onoD1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
E	Aldedh_2nd	e2onoE2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
E	Aldedh_1st_1	e2onoE1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
F	Aldedh_2nd	e2onoF2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
F	Aldedh_1st_1	e2onoF1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
G	Aldedh_2nd	e2onoG2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
G	Aldedh_1st_1	e2onoG1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
H	Aldedh_2nd	e2onoH1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
H	Aldedh_1st_1	e2onoH2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
B	Aldedh_2nd	e2onoB2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
B	Aldedh_1st_1	e2onoB1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
A	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
C	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
C	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
D	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
D	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
E	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
E	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
F	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
F	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
G	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
G	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
H	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
H	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
B	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
B	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF00171	Aldehyde dehydrogenase family (Aldedh)	Aldehyde dehydrogenase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	Aldehyde dehydrogenase	oxidoreductase 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 hydrolase activity, acting on ester bonds carboxylesterase activity carboxylic ester hydrolase activity hydrolase activity aldehyde dehydrogenase (NAD+) activity NAD binding binding nucleoside phosphate binding purine nucleotide binding oxidoreductase 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 hydrolase activity, acting on ester bonds carboxylesterase activity carboxylic ester hydrolase activity hydrolase activity aldehyde dehydrogenase (NAD+) activity NAD binding binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding small molecule binding phenylacetaldehyde dehydrogenase (NAD+) activity electron transfer activity	regulation of cellular process organic hydroxy compound metabolic process dopamine metabolic process catechol-containing compound metabolic process regulation of primary metabolic process biogenic amine biosynthetic process catecholamine metabolic process dopamine biosynthetic process catecholamine biosynthetic process catechol-containing compound biosynthetic process regulation of dopamine metabolic process regulation of biosynthetic process regulation of biological process regulation of amine metabolic process regulation of cellular process organic hydroxy compound metabolic process dopamine metabolic process catechol-containing compound metabolic process regulation of primary metabolic process biogenic amine biosynthetic process catecholamine metabolic process dopamine biosynthetic process catecholamine biosynthetic process catechol-containing compound biosynthetic process regulation of dopamine metabolic process regulation of biosynthetic process regulation of biological process regulation of amine metabolic process biological regulation primary metabolic process regulation of dopamine biosynthetic process amine metabolic process biosynthetic process amine biosynthetic process phenol-containing compound metabolic process organic hydroxy compound biosynthetic process phenol-containing compound biosynthetic process metabolic process cellular process regulation of catecholamine metabolic process regulation of metabolic process biogenic amine metabolic process carbohydrate metabolic process cellular response to stimulus cellular response to chemical stimulus response to stimulus response to chemical cellular response to xenobiotic stimulus nitroglycerin metabolic process xenobiotic metabolic process response to xenobiotic stimulus catabolic process aldehyde catabolic process aldehyde metabolic process alcohol catabolic process primary alcohol catabolic process alcohol metabolic process ethanol metabolic process organic hydroxy compound catabolic process ethanol catabolic process small molecule metabolic process small molecule catabolic process primary alcohol metabolic process serotonin metabolic process indole-containing compound metabolic process primary amino compound biosynthetic process primary amino compound metabolic process ammonium ion metabolic process indole-containing compound biosynthetic process regulation of serotonin biosynthetic process serotonin biosynthetic 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 membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR015590	Aldehyde dehydrogenase domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR016162	Aldehyde dehydrogenase, N-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR029510	Aldehyde dehydrogenase, glutamic acid active site	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H	IPR016163	Aldehyde dehydrogenase, C-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR016160	Aldehyde dehydrogenase, cysteine active site	Conserved Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H	Pharos: P05091	alcohol abuse esophageal squamous cell carcinoma vascular disease alcohol sensitivity, acute occupational dermatitis Liver Cirrhosis, Experimental male infertility colorectal cancer psoriasis asthma esophageal cancer perinatal necrotizing enterocolitis alcohol-induced disorders neoplasm of esophagus pancreatic intraductal papillary-mucinous neoplasm alcohol abuse esophageal squamous cell carcinoma vascular disease alcohol sensitivity, acute occupational dermatitis Liver Cirrhosis, Experimental male infertility colorectal cancer psoriasis asthma esophageal cancer perinatal necrotizing enterocolitis alcohol-induced disorders neoplasm of esophagus pancreatic intraductal papillary-mucinous neoplasm pituitary cancer gout primitive neuroectodermal tumor age-related macular degeneration heart disease wet macular degeneration alcohol-related disorders invasive ductal breast carcinoma B-cell chronic lymphocytic leukemia medulloblastoma breast fibroadenoma myocardial infarction non-alcoholic fatty liver disease ovarian cancer ductal breast carcinoma in situ pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia precancerous condition large cell medulloblastoma lung adenocarcinoma bipolar disorder carcinoma of esophagus necrotizing enterocolitis colorectal carcinoma non-small cell lung carcinoma pancreatic ductal adenocarcinoma glioblastoma alcohol dependence Wernicke-Korsakoff syndrome inherited disease susceptibility limb-girdle muscular dystrophy lung cancer atypical teratoid rhabdoid tumor malignant glioma breast carcinoma metabolic syndrome X chronic obstructive pulmonary disease

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.