2TPT
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Summary for 2TPT
Entry DOI | 10.2210/pdb2tpt/pdb |
Descriptor | THYMIDINE PHOSPHORYLASE, SULFATE ION (2 entities in total) |
Functional Keywords | thymidine phosphorylase, transferase, salvage pathway |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 47337.05 |
Authors | Pugmire, M.J.,Cook, W.J.,Jasanoff, A.,Walter, M.R.,Ealick, S.E. (deposition date: 1997-11-24, release date: 1999-03-02, Last modification date: 2024-02-21) |
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 (2.6 Å) |
Structure validation
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