STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
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STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE Descriptor: SULFATE ION, THYMIDINE PHOSPHORYLASE Authors: Pugmire, M.J, Cook, W.J, Jasanoff, A, Walter, M.R, Ealick, S.E. Deposit date: 1997-11-24 Release date: 1999-03-02 Last modified: 2024-02-21 Method: X-RAY DIFFRACTION (2.6 Å) Cite: Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J.Mol.Biol., 281, 1998
创建时间：
1997-11-24
