2V29
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT K15W)
Summary for 2V29
Entry DOI | 10.2210/pdb2v29/pdb |
Related | 1GT7 1OJR 2V2A 2V2B |
Descriptor | RHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | zinc enzyme, metal-binding, surface mutation, 2-ketose degradation, protein-protein interface, lyase, aldolase, class ii, rare sugar, cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone phosphate, bacterial l-rhamnose metabolism, rhamnose metabolism, protein engineering, domain motion for mechanical support of catalysis |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 2 |
Total formula weight | 61398.50 |
Authors | Grueninger, D.,Schulz, G.E. (deposition date: 2007-06-04, release date: 2008-01-08, Last modification date: 2023-12-13) |
Primary citation | Grueninger, D.,Schulz, G.E. Antenna Domain Mobility and Enzymatic Reaction of L-Rhamnulose-1-Phosphate Aldolase. Biochemistry, 47:607-, 2008 Cited by PubMed: 18085797DOI: 10.1021/BI7012799 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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