1QDS
SUPERSTABLE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE (TIM)
Summary for 1QDS
Entry DOI | 10.2210/pdb1qds/pdb |
Related | 1AMK |
Descriptor | TRIOSEPHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID (3 entities in total) |
Functional Keywords | tim, leishmania, stability, mutagenesis, pka, isomerase |
Biological source | Leishmania mexicana |
Cellular location | Cytoplasm: P48499 |
Total number of polymer chains | 1 |
Total formula weight | 27364.27 |
Authors | Lambeir, A.M.,Backmann, J.,Ruiz-Sanz, J.,Filimonov, V.,Nielsen, J.E.,Vriend, G.,Kursula, I.,Norledge, B.V.,Wierenga, R.K. (deposition date: 1999-07-10, release date: 2000-12-13, Last modification date: 2024-02-14) |
Primary citation | Lambeir, A.M.,Backmann, J.,Ruiz-Sanz, J.,Filimonov, V.,Nielsen, J.E.,Kursula, I.,Norledge, B.V.,Wierenga, R.K. The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase. Eur.J.Biochem., 267:2516-2524, 2000 Cited by PubMed: 10785370DOI: 10.1046/j.1432-1327.2000.01254.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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