| 1ENZ | Oxidoreductase | date | Jan 27, 1995 ![]() |
||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 Mutation: S94a |
Organism_scientific: Mycobacterium Tuberculosis Expression_system: Escherichia Coli | ||||||||||||||
| symmetry | Space Group: P 62 2 2 | R_factor | 0.193 | ||||||||||||
| crystal cell |
| ||||||||||||||
| method | X-Ray Diffraction | resolution | 2.7 Å | ||||||||||||
| ligand | NAD | enzyme |
| ||||||||||||
| 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 |
| ||||||||||||||
| 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 1ENZ in 3D |
|
|
| Visual 3D analysis of 1ENZ |
|
|
| Structure-derived information |
- Domain d1enz__, region [Jmol] [rasmolscript] [script source] |
| Sequence-derived information |
| Other resources with information on 1ENZ |
| Movements, Movies and Images |