6O4H

Structure of ALDH7A1 mutant A171V complexed with NAD

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	d6o4ha1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d6o4ha2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d6o4hc1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d6o4hc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d6o4hd1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d6o4hd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d6o4he1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d6o4he2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d6o4hg1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d6o4hg2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d6o4hb1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d6o4hb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d6o4hf1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d6o4hf2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d6o4hh1	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d6o4hh2	Artifacts	Tags	Tags	Tags	N-terminal Tags	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	8065638	3001479	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ALDH-like	8065638	3001479	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ALDH-like	8065638	3001479	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	ALDH-like	8065638	3001479	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	ALDH-like	8065638	3001479	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ALDH-like	8065638	3001479	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	ALDH-like	8065638	3001479	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	ALDH-like	8065638	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	e6o4hA2	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	e6o4hA1	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	e6o4hC1	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	e6o4hC2	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	e6o4hD2	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	e6o4hD1	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	e6o4hE2	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	e6o4hE1	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	e6o4hG2	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	e6o4hG1	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	e6o4hB1	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	e6o4hB2	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	e6o4hF1	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	e6o4hF2	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	e6o4hH2	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	e6o4hH1	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 (utative)
A	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)
C	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (utative)
C	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)
D	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (utative)
D	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)
E	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (utative)
E	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)
G	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (utative)
G	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)
B	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (utative)
B	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)
F	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (utative)
F	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)
H	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (utative)
H	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (utative)

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	Alpha-aminoadipic semialdehyde dehydrogenase	oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor aldehyde dehydrogenase (NAD+) activity aldehyde dehydrogenase [NAD(P)+] activity L-aminoadipate-semialdehyde dehydrogenase activity betaine-aldehyde dehydrogenase (NAD+) activity identical protein binding protein binding binding	metabolic process cellular process aldehyde metabolic process multicellular organismal process system process sensory perception nervous system process sensory perception of sound sensory perception of mechanical stimulus amino-acid betaine biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process amino-acid betaine metabolic process glycine betaine metabolic process metabolic process cellular process aldehyde metabolic process multicellular organismal process system process sensory perception nervous system process sensory perception of sound sensory perception of mechanical stimulus amino-acid betaine biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process amino-acid betaine metabolic process glycine betaine metabolic process glycine betaine biosynthetic process from choline ammonium ion metabolic process biosynthetic process choline metabolic process glycine betaine biosynthetic process amine metabolic process catabolic process choline catabolic process biogenic amine catabolic process amine catabolic 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 membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen nucleus

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	IPR044638	Aldehyde dehydrogenase family 7 member A1-like	Family
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

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: P49419	pyridoxine-dependent epilepsy bone disease coloboma osteoporosis acute myeloid leukemia breast carcinoma colorectal cancer Disease Exacerbation epilepsy gastric cancer intellectual disability chronic kidney disease gastric neoplasm pyridoxine-dependent epilepsy caused by ALDH7A1 mutant breast cancer pyridoxine-dependent epilepsy bone disease coloboma osteoporosis acute myeloid leukemia breast carcinoma colorectal cancer Disease Exacerbation epilepsy gastric cancer intellectual disability chronic kidney disease gastric neoplasm pyridoxine-dependent epilepsy caused by ALDH7A1 mutant breast cancer cystic fibrosis disorder of glutamate decarboxylase erectile dysfunction hereditary diffuse gastric adenocarcinoma

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.