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: 18562316 DOI: 10.1074/JBC.M802145200 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.85 Å)

Structure validation