2B35

Crystal structure of Mycobacterium tuberculosis enoyl reductase (InhA) inhibited by triclosan

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	d2b35a_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
B	d2b35b_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
C	d2b35c_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
D	d2b35d_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
E	d2b35e_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
F	d2b35f_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Enoyl-ACP reductase	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	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	8054262	3000038	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SDR-like	8054262	3000038	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SDR-like	8054262	3000038	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SDR-like	8054262	3000038	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	SDR-like	8054262	3000038	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	SDR-like	8054262	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	e2b35A1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
B	adh_short_C2	e2b35B1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
C	adh_short_C2	e2b35C1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
D	adh_short_C2	e2b35D1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
E	adh_short_C2	e2b35E1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
F	adh_short_C2	e2b35F1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	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 (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
D	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
E	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
F	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	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	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, C, D, E A, B, C, D, E, F	Enoyl-[acyl-carrier-protein] reductase [NADH]	fatty acid binding organic acid binding binding ion binding anion binding lipid binding carboxylic acid binding monocarboxylic acid binding small molecule binding NAD+ binding NAD binding nucleotide binding nucleoside phosphate binding purine nucleotide binding fatty acid binding organic acid binding binding ion binding anion binding lipid binding carboxylic acid binding monocarboxylic acid binding small molecule binding NAD+ binding NAD binding nucleotide binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding heterocyclic compound binding oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor trans-2-enoyl-CoA reductase (NADH) activity oxidoreductase activity, acting on the CH-CH group of donors catalytic activity enoyl-[acyl-carrier-protein] reductase (NADH) activity enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H)	oxoacid metabolic process cellular biosynthetic process cell wall organization or biogenesis lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process cellular component biogenesis mycolic acid biosynthetic process Actinobacterium-type cell wall biogenesis small molecule metabolic process cellular component organization or biogenesis peptidoglycan-based cell wall biogenesis fatty acid metabolic process oxoacid metabolic process cellular biosynthetic process cell wall organization or biogenesis lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process cellular component biogenesis mycolic acid biosynthetic process Actinobacterium-type cell wall biogenesis small molecule metabolic process cellular component organization or biogenesis peptidoglycan-based cell wall biogenesis fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process mycolic acid metabolic process carboxylic acid metabolic process primary metabolic process fatty acid biosynthetic process macromolecule biosynthetic process cell wall biogenesis biosynthetic process cell wall macromolecule biosynthetic process cellular lipid metabolic process cellular process metabolic process macromolecule metabolic process monocarboxylic acid metabolic process lipid metabolic process fatty acid elongation response to stimulus response to chemical response to antibiotic	cell periphery plasma membrane membrane cellular anatomical entity external encapsulating structure cell wall peptidoglycan-based cell wall

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR053410	Mycobacterial enoyl-ACP reductase	Family
A, B, C, D, E A, B, C, D, E, F	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.