1BID

E. COLI THYMIDYLATE SYNTHASE COMPLEXED WITH DUMP

Summary for 1BID

Entry DOI	10.2210/pdb1bid/pdb
Descriptor	THYMIDYLATE SYNTHASE, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (3 entities in total)
Functional Keywords	transferase (methyltransferase), substrate modules, methyltransferase
Biological source	Escherichia coli
Cellular location	Cytoplasm: P0A884
Total number of polymer chains	1
Total formula weight	30851.84
Authors	Stout, T.J.,Sage, C.R.,Stroud, R.M. (deposition date: 1997-06-27, release date: 1998-07-01, Last modification date: 2023-08-02)
Primary citation	Stout, T.J.,Sage, C.R.,Stroud, R.M. The additivity of substrate fragments in enzyme-ligand binding. Structure, 6:839-848, 1998 Cited by PubMed Abstract: Enzymes have evolved to recognise their target substrates with exquisite selectivity and specificity. Whether fragments of the substrate--perhaps never available to the evolving enzyme--are bound in the same manner as the parent substrate addresses the fundamental basis of specificity. An understanding of the relative contributions of individual portions of ligand molecules to the enzyme-binding interaction may offer considerable insight into the principles of substrate recognition. PubMed: 9687366 DOI: 10.1016/S0969-2126(98)00086-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation