1P44	Oxidoreductase	date	Apr 21, 2003
title	Targeting Tuberculosis And Malaria Through Inhibition Of Enoyl Reductase: Compound Activity And Structural Data
authors	M.R.Kuo, H.R.Morbidoni, D.Alland, S.F.Sneddon, B.B.Gourlie, M.M.Staveski, M.Leonard, J.S.Gregory, A.D.Janjigian, C.Yee, J.M.Musser, B.Kreiswirth, H.Iwamoto, R.Perozzo, W.R.Jacobs Jr, J.C.Sacchettini, D.A.Fidock, Tb Structural Genomics Consortium (Tbsgc)
compound		source
Molecule: Enoyl-[Acyl-Carrier-Protein] Reductase [Nadh] Chain: A, B, C, D, E, F Synonym: Nadh-Dependent Enoyl-Acp Reductase Ec: 1.3.1.9 Engineered: Yes		Organism_scientific: Mycobacterium Tuberculosis Gene: Inha Or Rv1484 Or Mt1531 Or Mtcy277.05 Or Mb1520 Expression_system: Escherichia Coli Expression_system_common: Bacteria
symmetry	Space Group: C 1 2 1	R_factor	0.190
crystal cell	length a length b length c angle alpha angle beta angle gamma 100.619 83.219 192.972 90.00 94.95 90.00
method	X-Ray Diffraction	resolution	2.70 Å
ligand	GEQ, NAD	enzyme	Enoyl-[acyl-carrier-protein] reductase (NADH);. Enoyl-[acyl carrier protein] reductase;. Enoyl-ACP reductase;. NADH-enoyl acyl carrier protein reductase;. NADH-specific enoyl-ACP reductase;. Enoyl-[acyl-carrier-protein] reductase (NADH2). Oxidoreductase E.C.1.3.1.9 BRENDA
similarity	Fabisubfamily. Belongs to the short-chain dehydrogenases/reductases (sdr) family.
subunit	Homotetramer.
catalytic activ.	Acyl-[acyl-carrier protein] + nad(+) = trans- 2,3-dehydroacyl-[acyl-carrier protein] + nadh.
pathway	Second reductive step in fatty acid biosynthesis. This isozyme is involved in mycolic acid biosynthesis.
genes	fabI (E. coli); fabI (H. pylori); MT1531, inhA (M. tuberculosis)
function	Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide.
Gene Ontology	Chain Function Process Component F, A, D, C, E, B enoyl-[acyl-carrier-protein]... oxidoreductase activity fatty acid biosynthetic proc... metabolic process lipid biosynthetic process response to antibiotic
Primary reference	Targeting tuberculosis and malaria through inhibition of Enoyl reductase: compound activity and structural data., Kuo MR, Morbidoni HR, Alland D, Sneddon SF, Gourlie BB, Staveski MM, Leonard M, Gregory JS, Janjigian AD, Yee C, Musser JM, Kreiswirth B, Iwamoto H, Perozzo R, Jacobs WR Jr, Sacchettini JC, Fidock DA, J Biol Chem 2003 Jun 6;278(23):20851-9. Epub 2003 Feb 26. PMID:12606558

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (287 Kb) [Save to disk] Biological Unit Coordinates (1p44.pdb1.gz) 172 Kb Biological Unit Coordinates (1p44.pdb2.gz) 168 Kb CSU: Contacts of Structural Units for 1P44 Likely Quarternary Molecular Structure file(s) for 1P44 Structure Factors (689 Kb) Retrieve 1P44 in mmCIF format [Save to disk]

View 1P44 in 3D

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Visual 3D analysis of 1P44

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1P44, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1p44a_, region A [Jmol] [rasmolscript] [script source]     - Domain d1p44b_, region B [Jmol] [rasmolscript] [script source]     - Domain d1p44c_, region C [Jmol] [rasmolscript] [script source]     - Domain d1p44d_, region D [Jmol] [rasmolscript] [script source]     - Domain d1p44e_, region E [Jmol] [rasmolscript] [script source]     - Domain d1p44f_, region F [Jmol] [rasmolscript] [script source] Fold representative 1p44 from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1p44_C] [1p44_D] [1p44_B] [1p44_F] [1p44_E] [1p44_A]

Other resources with information on 1P44

InterPro: IPR002347 MMDB (Entrez's Structure Database)

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