2V9L

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- E192A)

Summary for 2V9L

Entry DOI	10.2210/pdb2v9l/pdb
Related	1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V2B 2V9E 2V9F 2V9G 2V9I 2V9M 2V9N 2V9O
Descriptor	RHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, PHOSPHATE ION, ... (6 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
Total number of polymer chains	1
Total formula weight	31156.72
Authors	Grueninger, D.,Schulz, G.E. (deposition date: 2007-08-24, 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: 18187656 DOI: 10.1126/SCIENCE.1150421 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.23 Å)

Structure validation