3IT4
The Crystal Structure of Ornithine Acetyltransferase from Mycobacterium tuberculosis (Rv1653) at 1.7 A
Summary for 3IT4
Entry DOI | 10.2210/pdb3it4/pdb |
Descriptor | Arginine biosynthesis bifunctional protein argJ alpha chain, Arginine biosynthesis bifunctional protein argJ beta chain, GLYCEROL, ... (6 entities in total) |
Functional Keywords | mycobacterium tuberculosis, ornithine acetyltransferase, structural genomics, tb structural genomics consortium (tbsgc), acyltransferase, amino-acid biosynthesis, arginine biosynthesis, cytoplasm, multifunctional enzyme, transferase |
Biological source | Mycobacterium tuberculosis More |
Cellular location | Cytoplasm (Probable): P63571 P63571 |
Total number of polymer chains | 4 |
Total formula weight | 82856.85 |
Authors | Sankaranarayanan, R.,Cherney, M.M.,Garen, C.,Garen, G.,Yuan, M.,James, M.N.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2009-08-27, release date: 2010-03-02, Last modification date: 2023-09-06) |
Primary citation | Sankaranarayanan, R.,Cherney, M.M.,Garen, C.,Garen, G.,Niu, C.,Yuan, M.,James, M.N. The molecular structure of ornithine acetyltransferase from Mycobacterium tuberculosis bound to ornithine, a competitive inhibitor. J.Mol.Biol., 397:979-990, 2010 Cited by PubMed: 20184895DOI: 10.1016/j.jmb.2010.02.018 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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