2V9G
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- L84W-E192A)
Summary for 2V9G
Entry DOI | 10.2210/pdb2v9g/pdb |
Related | 1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V2B 2V9E 2V9F 2V9I 2V9L 2V9M |
Descriptor | RHAMNULOSE-1-PHOSPHATE ALDOLASE, L(+)-TARTARIC ACID, ZINC ION, ... (4 entities in total) |
Functional Keywords | zinc, lyase, aldolase, class ii, cytoplasm, protein engineering, 2-ketose degradation, cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism, metal-binding, oligomerization, interface design, protein-protein interface, rare sugar, aggregation, zinc enzyme, fibrillation, surface mutation, rhamnose metabolism |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 4 |
Total formula weight | 121909.94 |
Authors | Grueninger, D.,Schulz, G.E. (deposition date: 2007-08-23, release date: 2008-01-22, Last modification date: 2023-12-13) |
Primary citation | Grueninger, D.,Treiber, N.,Ziegler, M.O.P.,Koetter, J.W.A.,Schulze, M.-S.,Schulz, G.E. Designed Protein-Protein Association. Science, 319:206-, 2008 Cited by PubMed: 18187656DOI: 10.1126/SCIENCE.1150421 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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