1TPT
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![BU of 1tpt by Molmil](/molmil-images/mine/1tpt) | THREE-DIMENSIONAL STRUCTURE OF THYMIDINE PHOSPHORYLASE FROM ESCHERICHIA COLI AT 2.8 ANGSTROMS RESOLUTION | Descriptor: | SULFATE ION, THYMIDINE PHOSPHORYLASE, THYMINE | Authors: | Walter, M.R, Cook, W.J, Cole, L.B, Short, S.A, Koszalka, G.W, Krenitsky, T.A, Ealick, S.E. | Deposit date: | 1990-06-14 | Release date: | 1991-07-15 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. J.Biol.Chem., 265, 1990
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1AZY
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![BU of 1azy by Molmil](/molmil-images/mine/1azy) | STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE | Descriptor: | THYMIDINE PHOSPHORYLASE | Authors: | Pugmire, M.J, Cook, W.J, Jasanoff, A, Walter, M.R, Ealick, S.E. | Deposit date: | 1997-11-24 | Release date: | 1999-01-13 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (3 Å) | Cite: | Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J.Mol.Biol., 281, 1998
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1ECP
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![BU of 1ecp by Molmil](/molmil-images/mine/1ecp) | PURINE NUCLEOSIDE PHOSPHORYLASE | Descriptor: | PURINE NUCLEOSIDE PHOSPHORYLASE | Authors: | Mao, C, Ealick, S.E. | Deposit date: | 1995-07-13 | Release date: | 1996-06-20 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology. Structure, 5, 1997
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2TPT
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![BU of 2tpt by Molmil](/molmil-images/mine/2tpt) | 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
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