1CI7
TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII
Summary for 1CI7
Entry DOI | 10.2210/pdb1ci7/pdb |
Descriptor | PROTEIN (THYMIDYLATE SYNTHASE), 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, ... (4 entities in total) |
Functional Keywords | methyltransferase, nucleotide biosynthesis, half-sites reactivity, transferase |
Biological source | Pneumocystis carinii |
Total number of polymer chains | 2 |
Total formula weight | 69900.40 |
Authors | Anderson, A.C.,O'Neil, R.H.,Delano, W.L.,Stroud, R.M. (deposition date: 1999-04-08, release date: 2000-04-10, Last modification date: 2024-04-03) |
Primary citation | Anderson, A.C.,O'Neil, R.H.,DeLano, W.L.,Stroud, R.M. The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits. Biochemistry, 38:13829-13836, 1999 Cited by PubMed: 10529228DOI: 10.1021/bi991610i PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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