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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>

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PDB ID2v2b  sequence information (FASTA format)   
RELATED PDB ID2uyu, 2v9n, 2v29, 2uyv, 2v9g, 2v9e, 1gt7, 2v9l, 2v2a, 2v9m, 2v9f, 1ojr, 2v9o, 2v9i
DescriptorRHAMNULOSE-1-PHOSPHATE ALDOLASE (E.C.4.1.2.19)
TitleL-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E117S-E192A-K248G-R253A-E254A)
Functional KeywordsZINC ENZYME, METAL-BINDING, SURFACE MUTATION, 2-KETOSE DEGRADATION, PROTEIN-PROTEIN INTERFACE, ZINC, 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 sourceESCHERICHIA COLI
Cellular location [UNP - P32169] Cytoplasm
Total number of polymer chains1
Total molecular weight30219.2 (the details in Structural Details Page)
AuthorsGrueninger, D. , Schulz, G.E. (deposition date : 2007-06-04, release date : 2008-01-08)
Primary citationGrueninger, D. , Schulz, G.E.
Antenna Domain Mobility and Enzymatic Reaction of L-Rhamnulose-1-Phosphate Aldolase.
Biochemistry, 47:607 - , 2008.(PubMed : 18085797)  (DOI: 10.1021/bi7012799)
Experimental methodX-RAY DIFFRACTION ( 1.50[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P32169 ) , eF-site , KEGG ( EC 4.1.2.19 ) , PISA