2VOM
Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation.
Summary for 2VOM
Entry DOI | 10.2210/pdb2vom/pdb |
Related | 1HTI 1WYI |
Descriptor | TRIOSEPHOSPHATE ISOMERASE (2 entities in total) |
Functional Keywords | isomerase, alternative splicing, fatty acid biosynthesis, lipid synthesis, disease mutation, pentose shunt, phosphoprotein, gluconeogenesis, glycolysis, acetylation, polymorphism |
Biological source | HOMO SAPIENS (HUMAN) |
Total number of polymer chains | 4 |
Total formula weight | 106801.49 |
Authors | Rodriguez-Almazan, C.,Arreola-Alemon, R.,Rodriguez-Larrea, D.,Aguirre-Lopez, B.,de Gomez-Puyou, M.T.,Perez-Montfort, R.,Costas, M.,Gomez-Puyou, A.,Torres-Larios, A. (deposition date: 2008-02-19, release date: 2008-06-17, Last modification date: 2023-12-13) |
Primary citation | Rodriguez-Almazan, C.,Arreola-Alemon, R.,Rodriguez-Larrea, D.,Aguirre-Lopez, B.,De Gomez-Puyou, M.T.,Perez-Montfort, R.,Costas, M.,Gomez-Puyou, A.,Torres-Larios, A. Structural Basis of Human Triosephosphate Isomerase Deficiency: Mutation E104D is Related to Alterations of a Conserved Water Network at the Dimer Interface. J.Biol.Chem., 283:23254-, 2008 Cited by PubMed: 18562316DOI: 10.1074/JBC.M802145200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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