2V2H
The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM
Summary for 2V2H
Entry DOI | 10.2210/pdb2v2h/pdb |
Related | 1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 2J24 2J27 2V0T 2V2C 2V2D 3TIM 4TIM 5TIM 6TIM |
Descriptor | TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL, 2-PHOSPHOGLYCOLIC ACID, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | gluconeogenesis, lipid synthesis, 2-phospho glycolate, glycolysis, engineering, pentose shunt, point mutation, tim, 2pg, a178l, loop6, hinge, loop-6, enzyme, fatty acid biosynthesis, triosephosphate isomerase, isomerase, glycosome, monomeric, tim-barrel |
Biological source | TRYPANOSOMA BRUCEI BRUCEI |
Total number of polymer chains | 3 |
Total formula weight | 78801.92 |
Authors | Alahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K. (deposition date: 2007-06-06, release date: 2008-02-19, Last modification date: 2024-05-01) |
Primary citation | Alahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K. Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed-Like Conformation in Dimeric and Monomeric Tim. Acta Crystallogr.,Sect.D, 64:178-, 2008 Cited by PubMed: 18219118DOI: 10.1107/S0907444907059021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.18 Å) |
Structure validation
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