6AHE

Crystal structure of enoyl-ACP reductase from Acinetobacter baumannii in complex with NAD and AFN-1252

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6ahea_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	automated matches	Acinetobacter baumannii ATCC 19606 (Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)
B [auth D]	d6ahed_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	automated matches	Acinetobacter baumannii ATCC 19606 (Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)
C	d6ahec_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	automated matches	Acinetobacter baumannii ATCC 19606 (Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)
D [auth B]	d6aheb_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	automated matches	Acinetobacter baumannii ATCC 19606 (Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	SDR-like	8094683	3000038	SCOP2B (2022-06-29)
B [auth D]	SCOP2 Family	Short-chain dehydrogenases/reductases, SDR	8094682	4000029	SCOP2 (2022-06-29)
B [auth D]	SCOP2 Superfamily	SDR-like	8094683	3000038	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	SDR-like	8094683	3000038	SCOP2B (2022-06-29)
D [auth B]	SCOP2B Superfamily	SDR-like	8094683	3000038	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	adh_short_C2_1	e6aheA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
B [auth D]	adh_short_C2_1	e6aheD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
C	adh_short_C2_1	e6aheC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
D [auth B]	adh_short_C2_1	e6aheB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
B [auth D]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
C	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)
D [auth B]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth D], C, D [auth B]	PF13561	Enoyl-(Acyl carrier protein) reductase (adh_short_C2)	Enoyl-(Acyl carrier protein) reductase	This domain is found in Enoyl-(Acyl carrier protein) reductases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth D], C, D [auth B]	Enoyl-[acyl-carrier-protein] reductase [NADH]	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding enoyl-[acyl-carrier-protein] reductase (NADH) activity oxidoreductase activity enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-CH group of donors catalytic activity	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth D], C, D [auth B]	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B [auth D], C, D [auth B]	IPR002347	Short-chain dehydrogenase/reductase SDR	Family
A, B [auth D], C, D [auth B]	IPR014358	Enoyl-[acyl-carrier-protein] reductase (NADH)	Family

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.