1zid
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1zid.gif|left|200px]] | + | [[Image:1zid.gif|left|200px]] |
- | + | ||
- | '''LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR''' | + | {{Structure |
+ | |PDB= 1zid |SIZE=350|CAPTION= <scene name='initialview01'>1zid</scene>, resolution 2.7Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZID:ISONICOTINIC-ACETYL-NICOTINAMIDE-ADENINE DINUCLEOTIDE'>ZID</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 1ZID is a [ | + | 1ZID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZID OCA]. |
==Reference== | ==Reference== | ||
- | Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis., Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC, Science. 1998 Jan 2;279(5347):98-102. PMID:[http:// | + | Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis., Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC, Science. 1998 Jan 2;279(5347):98-102. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9417034 9417034] |
[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]] | [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
Line 27: | Line 36: | ||
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
- | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: tb structural genomics consortium]] | [[Category: tb structural genomics consortium]] | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
[[Category: tuberculosis]] | [[Category: tuberculosis]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:35:50 2008'' |
Revision as of 13:35, 20 March 2008
| |||||||
, resolution 2.7Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | |||||||
Activity: | [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR
Overview
The preferred antitubercular drug isoniazid specifically targets a long-chain enoyl-acyl carrier protein reductase (InhA), an enzyme essential for mycolic acid biosynthesis in Mycobacterium tuberculosis. Despite the widespread use of this drug for more than 40 years, its precise mode of action has remained obscure. Data from x-ray crystallography and mass spectrometry reveal that the mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of InhA.
About this Structure
1ZID is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis., Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC, Science. 1998 Jan 2;279(5347):98-102. PMID:9417034 [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
Page seeded by OCA on Thu Mar 20 15:35:50 2008
Categories: Mycobacterium tuberculosis | Single protein | Jr., W R.Jacobs. | Rozwarski, D A. | Sacchettini, J C. | TBSGC, TB Structural Genomics Consortium. | ZID | Enoyl-acp reductase | Inha enzyme | Isoniazid | Modified nadh | Mycolic acid biosynthesis | Oxidoreductase | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc | Tuberculosis