1ENY | Oxidoreductase | date | Jan 27, 1995 | ||||||||||||
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authors | A.Dessen, A.Quemard, J.S.Blanchard, W.R.Jacobs Jr., J.C.Sacchettini, Tb Structural Genomics Consortium (Tbsgc) | ||||||||||||||
compound | source | ||||||||||||||
Molecule: Enoyl-Acyl Carrier Protein (Acp) Reductase Chain: Null Synonym: Inha Engineered: Yes |
Organism_scientific: Mycobacterium Tuberculosis Expression_system: Escherichia Coli | ||||||||||||||
symmetry | Space Group: P 62 2 2 | R_factor | 0.196 | ||||||||||||
crystal cell |
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method | X-Ray Diffraction | resolution | 2.2 Å | ||||||||||||
ligand | NAD | enzyme |
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note | 1ENY is a representative structure | ||||||||||||||
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 | MT1531, inhA (M. tuberculosis) | ||||||||||||||
function | Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide. | ||||||||||||||
Gene Ontology |
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Primary reference | Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis., Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC, Science 1995 Mar 17;267(5204):1638-41. PMID:7886450 |
Data retrieval |
View 1ENY in 3D |
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Visual 3D analysis of 1ENY |
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Structure-derived information |
- Domain d1eny__, region [Jmol] [rasmolscript] [script source] |
Sequence-derived information |
Other resources with information on 1ENY |
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