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: 25427005 DOI: 10.1021/jm5011176 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation