1AMK
LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE
Summary for 1AMK
Entry DOI | 10.2210/pdb1amk/pdb |
Descriptor | TRIOSE PHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID (3 entities in total) |
Functional Keywords | tim, 2-pg, pga, gluconeogenesis, fatty acid biosynthesis |
Biological source | Leishmania mexicana |
Cellular location | Cytoplasm: P48499 |
Total number of polymer chains | 1 |
Total formula weight | 27365.25 |
Authors | Williams, J.C.,Wierenga, R. (deposition date: 1997-06-17, release date: 1997-12-17, Last modification date: 2024-05-22) |
Primary citation | Williams, J.C.,Zeelen, J.P.,Neubauer, G.,Vriend, G.,Backmann, J.,Michels, P.A.,Lambeir, A.M.,Wierenga, R.K. Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Protein Eng., 12:243-250, 1999 Cited by PubMed: 10235625DOI: 10.1093/protein/12.3.243 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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