2YCE
Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.
Replaces: 1W8RSummary for 2YCE
Entry DOI | 10.2210/pdb2yce/pdb |
Related | 1OJX 1OK4 1OK6 1W8S |
Descriptor | FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1, D-MANNITOL-1,6-DIPHOSPHATE (3 entities in total) |
Functional Keywords | lyase, glycolysis |
Biological source | THERMOPROTEUS TENAX |
Total number of polymer chains | 10 |
Total formula weight | 290831.96 |
Authors | Lorentzen, E.,Siebers, B.,Hensel, R.,Pohl, E. (deposition date: 2011-03-14, release date: 2011-04-27, Last modification date: 2023-12-20) |
Primary citation | Lorentzen, E.,Siebers, B.,Hensel, R.,Pohl, E. Mechanism of the Schiff Base Forming Fructose-1,6-Bisphosphate Aldolase: Structural Analysis of Reaction Intermediates. Biochemistry, 44:4222-, 2005 Cited by PubMed: 15766250DOI: 10.1021/BI048192O PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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