2V9F
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)
Summary for 2V9F
Entry DOI | 10.2210/pdb2v9f/pdb |
Related | 1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V2B 2V9E 2V9G 2V9I 2V9L 2V9M |
Descriptor | RHAMNULOSE-1-PHOSPHATE ALDOLASE, ACETATE ION, ZINC ION, ... (4 entities in total) |
Functional Keywords | entropy index, metal-binding, oligomerization, zinc, lyase, aldolase, class ii, cytoplasm, cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism, interface design, surface mutation, 2-ketose degradation, protein-protein interface, rare sugar, aggregation, zinc enzyme, fibrillation, rhamnose metabolism, protein engineering |
Biological source | ESCHERICHIA COLI |
Cellular location | Cytoplasm: P32169 |
Total number of polymer chains | 1 |
Total formula weight | 30621.80 |
Authors | Grueninger, D.,Schulz, G.E. (deposition date: 2007-08-23, release date: 2008-01-15, 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 (2.1 Å) |
Structure validation
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