2V2B

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E117S- E192A-K248G-R253A-E254A)

Summary for 2V2B

Entry DOI	10.2210/pdb2v2b/pdb
Related	1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V9E 2V9F 2V9G 2V9I 2V9L 2V9M 2V9N 2V9O
Descriptor	RHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, ACETATE ION, ... (6 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
Cellular location	Cytoplasm: P32169
Total number of polymer chains	1
Total formula weight	30218.98
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: 18085797 DOI: 10.1021/BI7012799 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation