1G1L
THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-GLUCOSE COMPLEX.
Summary for 1G1L
Entry DOI | 10.2210/pdb1g1l/pdb |
Related | 1fxo 1fzw 1g0r 1g23 1g2v 1g31 |
Descriptor | GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE, SULFATE ION, 2'DEOXY-THYMIDINE-5'-DIPHOSPHO-ALPHA-D-GLUCOSE, ... (5 entities in total) |
Functional Keywords | l-rhamnose, nucleotidyltransferase, pyrophosphorylase, thymidylyltransferase, allostery, transferase |
Biological source | Pseudomonas aeruginosa |
Total number of polymer chains | 8 |
Total formula weight | 271533.71 |
Authors | Blankenfeldt, W.,Asuncion, M.,Lam, J.S.,Naimsmith, J.H. (deposition date: 2000-10-12, release date: 2000-12-27, Last modification date: 2018-01-31) |
Primary citation | Blankenfeldt, W.,Asuncion, M.,Lam, J.S.,Naismith, J.H. The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA). EMBO J., 19:6652-6663, 2000 Cited by PubMed: 11118200DOI: 10.1093/emboj/19.24.6652 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
Download full validation report