4E0C
1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)
Summary for 4E0C
Entry DOI | 10.2210/pdb4e0c/pdb |
Related | 3IGX 3TE9 3TK7 3TKF 3TNO 3UPB |
Descriptor | Transaldolase, MAGNESIUM ION, ACETATE ION, ... (4 entities in total) |
Functional Keywords | structural genomics, niaid, national institute of allergy and infectious diseases, center for structural genomics of infectious diseases, csgid, alpha-beta barrel/tim barrel, transferase |
Biological source | Francisella tularensis subsp. tularensis |
Cellular location | Cytoplasm (By similarity): Q5NFX0 |
Total number of polymer chains | 2 |
Total formula weight | 77035.50 |
Authors | Light, S.H.,Minasov, G.,Halavaty, A.S.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2012-03-02, release date: 2012-03-14, Last modification date: 2023-09-13) |
Primary citation | Light, S.H.,Minasov, G.,Duban, M.E.,Anderson, W.F. Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes. Acta Crystallogr.,Sect.D, 70:544-552, 2014 Cited by PubMed: 24531488DOI: 10.1107/S1399004713030666 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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