6NLH
| Structure of human triose phosphate isomerase R189A | Descriptor: | BROMIDE ION, PHOSPHATE ION, SODIUM ION, ... | Authors: | Richards, K.R, Roland, B.P, Palladino, M.J, VanDemark, A.P. | Deposit date: | 2019-01-08 | Release date: | 2019-06-19 | Last modified: | 2023-10-11 | Method: | X-RAY DIFFRACTION (2.199 Å) | Cite: | Missense variant in TPI1 (Arg189Gln) causes neurologic deficits through structural changes in the triosephosphate isomerase catalytic site and reduced enzyme levels in vivo. Biochim Biophys Acta Mol Basis Dis, 1865, 2019
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4POC
| Structure of Triosephosphate Isomerase Wild Type human enzyme. | Descriptor: | BROMIDE ION, PHOSPHATE ION, POTASSIUM ION, ... | Authors: | Amrich, C.G, Aslam, A.A, Heroux, A, VanDemark, A.P. | Deposit date: | 2014-02-25 | Release date: | 2015-01-14 | Last modified: | 2023-09-20 | Method: | X-RAY DIFFRACTION (1.601 Å) | Cite: | Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency. Biochim.Biophys.Acta, 1852, 2015
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4POD
| Structure of Triosephosphate Isomerase I170V mutant human enzyme. | Descriptor: | BROMIDE ION, PHOSPHATE ION, POTASSIUM ION, ... | Authors: | Amrich, C.G, Aslam, A.A, Heroux, A, VanDemark, A.P. | Deposit date: | 2014-02-25 | Release date: | 2015-01-14 | Last modified: | 2023-09-20 | Method: | X-RAY DIFFRACTION (1.99 Å) | Cite: | Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency. Biochim.Biophys.Acta, 1852, 2015
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4ZVJ
| Structure of human triose phosphate isomerase K13M | Descriptor: | POTASSIUM ION, SODIUM ION, Triosephosphate isomerase | Authors: | Amrich, C.G, Smith, C, Heroux, A, VanDemark, A.P. | Deposit date: | 2015-05-18 | Release date: | 2016-03-09 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (1.6996 Å) | Cite: | Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency. Biochim. Biophys. Acta, 1852, 2015
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