1AZY
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Summary for 1AZY
| Entry DOI | 10.2210/pdb1azy/pdb |
| Descriptor | THYMIDINE PHOSPHORYLASE (1 entity in total) |
| Functional Keywords | glycosyltransferase, thymidine phosphorylase, salvage pathway |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 94481.98 |
| Authors | Pugmire, M.J.,Cook, W.J.,Jasanoff, A.,Walter, M.R.,Ealick, S.E. (deposition date: 1997-11-24, release date: 1999-01-13, Last modification date: 2024-02-07) |
| Primary citation | Pugmire, M.J.,Cook, W.J.,Jasanoff, A.,Walter, M.R.,Ealick, S.E. Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J.Mol.Biol., 281:285-299, 1998 Cited by PubMed: 9698549DOI: 10.1006/jmbi.1998.1941 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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