3V9H

Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352A

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	d3v9ha_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d3v9hb_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d3v9hc_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d3v9hd_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	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	8083604	3001479	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ALDH-like	8083604	3001479	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ALDH-like	8083604	3001479	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ALDH-like	8083604	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	e3v9hA1	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	e3v9hA2	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	e3v9hB1	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	e3v9hB2	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	e3v9hC2	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	e3v9hC1	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	e3v9hD1	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	e3v9hD2	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)
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)
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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	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	Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial	1-pyrroline-5-carboxylate dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic 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 electron transfer activity identical protein binding protein binding binding	oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process glutamine family amino acid metabolic process proteinogenic amino acid metabolic process proline metabolic process metabolic process small molecule metabolic process cellular process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process glutamine family amino acid metabolic process proteinogenic amino acid metabolic process proline metabolic process metabolic process small molecule metabolic process cellular process catabolic process glutamine family amino acid catabolic process organic acid catabolic process proline catabolic process cellular catabolic process carboxylic acid catabolic process glutamate metabolic process amino acid catabolic process proline catabolic process to glutamate dicarboxylic acid metabolic process L-amino acid catabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process small molecule catabolic process 4-hydroxyproline metabolic process non-proteinogenic amino acid metabolic process 4-hydroxyproline catabolic process non-proteinogenic amino acid catabolic process cellular modified amino acid metabolic process cellular modified amino acid catabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cytosol 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	IPR015590	Aldehyde dehydrogenase domain	Domain
A, B, C, D	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B, C, D	IPR016162	Aldehyde dehydrogenase, N-terminal	Homologous Superfamily
A, B, C, D	IPR029510	Aldehyde dehydrogenase, glutamic acid active site	Conserved Site
A, B, C, D	IPR005931	Delta-1-pyrroline-5-carboxylate dehydrogenase	Family
A, B, C, D	IPR016163	Aldehyde dehydrogenase, C-terminal	Homologous Superfamily
A, B, C, D	IPR016160	Aldehyde dehydrogenase, cysteine active site	Conserved Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P30038	hyperprolinemia type 2 hyperprolinemia atopic eczema interstitial cystitis medulloblastoma osteosarcoma Precancerous Conditions large cell medulloblastoma nephrosclerosis pancreatic ductal adenocarcinoma primitive neuroectodermal tumor esophageal adenocarcinoma intellectual disability lung cancer non-alcoholic fatty liver disease hyperprolinemia type 2 hyperprolinemia atopic eczema interstitial cystitis medulloblastoma osteosarcoma Precancerous Conditions large cell medulloblastoma nephrosclerosis pancreatic ductal adenocarcinoma primitive neuroectodermal tumor esophageal adenocarcinoma intellectual disability lung cancer non-alcoholic fatty liver disease precancerous condition psoriasis

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.