1YDV
TRIOSEPHOSPHATE ISOMERASE (TIM)
Summary for 1YDV
Entry DOI | 10.2210/pdb1ydv/pdb |
Descriptor | TRIOSEPHOSPHATE ISOMERASE (2 entities in total) |
Functional Keywords | isomerase, glycolysis, gluconeogenesis |
Biological source | Plasmodium falciparum (malaria parasite P. falciparum) |
Total number of polymer chains | 2 |
Total formula weight | 55995.48 |
Authors | Velankar, S.S.,Murthy, M.R.N. (deposition date: 1997-04-24, release date: 1997-10-15, Last modification date: 2024-04-03) |
Primary citation | Velanker, S.S.,Ray, S.S.,Gokhale, R.S.,Suma, S.,Balaram, H.,Balaram, P.,Murthy, M.R. Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. Structure, 5:751-761, 1997 Cited by PubMed Abstract: Malaria caused by the parasite Plasmodium falciparum is a major public health concern. The parasite lacks a functional tricarboxylic acid cycle, making glycolysis its sole energy source. Although parasite enzymes have been considered as potential antimalarial drug targets, little is known about their structural biology. Here we report the crystal structure of triosephosphate isomerase (TIM) from P. falciparum at 2.2 A resolution. PubMed: 9261072DOI: 10.1016/S0969-2126(97)00230-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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