Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1JG0

Crystal structure of Escherichia coli thymidylate synthase complexed with 2'-deoxyuridine-5'-monophosphate and N,O-didansyl-L-tyrosine

Summary for 1JG0
Entry DOI10.2210/pdb1jg0/pdb
Descriptorthymidylate synthase, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, N,O-DIDANSYL-L-TYROSINE, ... (4 entities in total)
Functional Keywordsthymidylate synthase, didansyl tyrosine, transferase
Biological sourceEscherichia coli
Cellular locationCytoplasm: P0A884
Total number of polymer chains2
Total formula weight62686.75
Authors
Fritz, T.A.,Tondi, D.,Finer-Moore, J.S.,Costi, M.P.,Stroud, R.M. (deposition date: 2001-06-22, release date: 2002-02-08, Last modification date: 2024-11-06)
Primary citationFritz, T.A.,Tondi, D.,Finer-Moore, J.S.,Costi, M.P.,Stroud, R.M.
Predicting and harnessing protein flexibility in the design of species-specific inhibitors of thymidylate synthase.
Chem.Biol., 8:981-995, 2001
Cited by
PubMed Abstract: Protein plasticity in response to ligand binding abrogates the notion of a rigid receptor site. Thus, computational docking alone misses important prospective drug design leads. Bacterial-specific inhibitors of an essential enzyme, thymidylate synthase (TS), were developed using a combination of computer-based screening followed by in-parallel synthetic elaboration and enzyme assay [Tondi et al. (1999) Chem. Biol. 6, 319-331]. Specificity was achieved through protein plasticity and despite the very high sequence conservation of the enzyme between species.
PubMed: 11590022
DOI: 10.1016/S1074-5521(01)00067-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

237423

数据于2025-06-11公开中

PDB statisticsPDBj update infoContact PDBjnumon