6NLH
Structure of human triose phosphate isomerase R189A
Summary for 6NLH
Entry DOI | 10.2210/pdb6nlh/pdb |
Descriptor | Triosephosphate isomerase, SODIUM ION, BROMIDE ION, ... (5 entities in total) |
Functional Keywords | isomerase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 8 |
Total formula weight | 210990.36 |
Authors | Richards, K.R.,Roland, B.P.,Palladino, M.J.,VanDemark, A.P. (deposition date: 2019-01-08, release date: 2019-06-19, Last modification date: 2023-10-11) |
Primary citation | Roland, B.P.,Richards, K.R.,Hrizo, S.L.,Eicher, S.,Barile, Z.J.,Chang, T.C.,Savon, G.,Bianchi, P.,Fermo, E.,Ricerca, B.M.,Tortorolo, L.,Vockley, J.,VanDemark, A.P.,Palladino, M.J. 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, 1865:2257-2266, 2019 Cited by PubMed: 31075491DOI: 10.1016/j.bbadis.2019.05.002 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.199 Å) |
Structure validation
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