3H9K
Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry
Summary for 3H9K
Entry DOI | 10.2210/pdb3h9k/pdb |
Related | 1HVY 1HW3 2RD8 2RDA |
Descriptor | Thymidylate synthase, 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | transferase, methyltransferase, nucleotide biosynthesis |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus : P04818 |
Total number of polymer chains | 5 |
Total formula weight | 179967.22 |
Authors | Gibson, L.M.,Lovelace, L.L.,Lebioda, L. (deposition date: 2009-04-30, release date: 2010-05-12, Last modification date: 2023-09-06) |
Primary citation | Gibson, L.M.,Celeste, L.R.,Lovelace, L.L.,Lebioda, L. Structures of human thymidylate synthase R163K with dUMP, FdUMP and glutathione show asymmetric ligand binding. Acta Crystallogr.,Sect.D, 67:60-66, 2011 Cited by PubMed: 21206062DOI: 10.1107/S0907444910044732 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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