4FGT
Allosteric peptidic inhibitor of human thymidylate synthase that stabilizes inactive conformation of the enzyme.
Summary for 4FGT
Entry DOI | 10.2210/pdb4fgt/pdb |
Related | 3EGY 3N5E |
Descriptor | Thymidylate synthase, CG peptide, SULFATE ION, ... (4 entities in total) |
Functional Keywords | dimer, mutant k47a of hts, inactive hts conformation, hts complex with peptidic inhibitor, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus : P04818 |
Total number of polymer chains | 2 |
Total formula weight | 38076.39 |
Authors | Tochowicz, A.,Finer-Moore, J.,Stroud, R.M.,Costi, M.P. (deposition date: 2012-06-04, release date: 2013-03-06, Last modification date: 2017-11-15) |
Primary citation | Tochowicz, A.,Santucci, M.,Saxena, P.,Guaitoli, G.,Trande, M.,Finer-Moore, J.,Stroud, R.M.,Costi, M.P. Alanine mutants of the interface residues of human thymidylate synthase decode key features of the binding mode of allosteric anticancer peptides. J.Med.Chem., 58:1012-1018, 2015 Cited by PubMed: 25427005DOI: 10.1021/jm5011176 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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