1W2H
Crystal Structure Of Mycobacterium Tuberculosis Thymidylate Kinase Complexed With Azidothymidine Monophosphate (AZT-MP) (2.0 A Resolution)
Summary for 1W2H
Entry DOI | 10.2210/pdb1w2h/pdb |
Related | 1G3U 1GSI 1GTV 1MRN 1MRS 1N5I 1N5J 1N5K 1N5L 1W2G |
Descriptor | THYMIDYLATE KINASE TMK, 3'-AZIDO-3'-DEOXYTHYMIDINE-5'-MONOPHOSPHATE, ACETATE ION, ... (4 entities in total) |
Functional Keywords | transferase, mycobacterium tuberculosis, thymidylate kinase, azt, inhibition mechanism |
Biological source | MYCOBACTERIUM TUBERCULOSIS |
Total number of polymer chains | 2 |
Total formula weight | 46543.85 |
Authors | Fioravanti, E.,Adam, V.,Munier-Lehmann, H.,Bourgeois, D. (deposition date: 2004-07-06, release date: 2005-01-12, Last modification date: 2023-12-13) |
Primary citation | Fioravanti, E.,Adam, V.,Munier-Lehmann, H.,Bourgeois, D. The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition. Biochemistry, 44:130-137, 2005 Cited by PubMed: 15628853DOI: 10.1021/bi0484163 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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