4OGD

Crystal structure of succinic semialdehyde dehydrogenase from Streptococcus pyogenes in complex with NADP+ as the cofactor

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d4ogdb_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	(Streptococcus pyogenes MGAS1882 ) [TaxId: 1010840 ],	SCOPe (2.08)
A	d4ogda_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	(Streptococcus pyogenes MGAS1882 ) [TaxId: 1010840 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	ALDH-like	8072441	3001479	SCOP2B (2022-06-29)
A	SCOP2 Family	ALDH-like	8072440	4000806	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ALDH-like	8072441	3001479	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Aldedh_2nd	e4ogdB2	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	e4ogdB1	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)
A	Aldedh_2nd	e4ogdA2	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	e4ogdA1	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)
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)
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)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Succinate-semialdehyde dehydrogenase	succinate-semialdehyde dehydrogenase (NADP+) activity oxidoreductase activity succinate-semialdehyde dehydrogenase [NAD(P)+] 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(P)+] activity succinate-semialdehyde dehydrogenase (NAD+) activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR047110	Succinate-semialdehyde dehydrogenase [NADP(+)] GABD/Sad-like	Family
A, B	IPR015590	Aldehyde dehydrogenase domain	Domain
A, B	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B	IPR016162	Aldehyde dehydrogenase, N-terminal	Homologous Superfamily
A, B	IPR016163	Aldehyde dehydrogenase, C-terminal	Homologous Superfamily
A, B	IPR044148	Succinate-semialdehyde dehydrogenase GabD1-like	Domain

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.