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2V9E

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)

Summary for 2V9E
Entry DOI10.2210/pdb2v9e/pdb
Related1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V2B 2V9F 2V9G 2V9I 2V9L 2V9M
DescriptorRHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, ACETATE ION, ... (4 entities in total)
Functional Keywordsentropy index, metal-binding, oligomerization, zinc, lyase, aldolase, class ii, cytoplasm, cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone, 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 sourceESCHERICHIA COLI
Cellular locationCytoplasm: P32169
Total number of polymer chains2
Total formula weight61066.47
Authors
Grueninger, D.,Schulz, G.E. (deposition date: 2007-08-23, release date: 2008-01-15, Last modification date: 2023-12-13)
Primary citationGrueninger, 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 (1.58 Å)
Structure validation

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