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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>

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PDB ID2pan  sequence information (FASTA format)   
DescriptorGlyoxylate carboligase (E.C.4.1.1.47)
TitleCrystal structure of E. coli glyoxylate carboligase
Functional Keywordsthiamin-diphosphate (ThDP), thimain-dependent enzymes, FAD, enzyme, glyoxylate carboligase, Lyase
Biological sourceEscherichia coli
Total number of polymer chains6
Total molecular weight419284.3 (the details in Structural Details Page)
AuthorsKaplun, A. , Chipman, D.M. , Barak, Z. , Vyazmensky, M. , Shaanan, B. (deposition date : 2007-03-27, release date : 2008-01-01)
Primary citationKaplun, A. , Binshtein, E. , Vyazmensky, M. , Steinmetz, A. , Barak, Z. , Chipman, D.M. , Tittmann, K. , Shaanan, B.
Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.
Nat.Chem.Biol., 4:113 - 118, 2008.(PubMed : 18176558)  (DOI: 10.1038/nchembio.62)
Experimental methodX-RAY DIFFRACTION ( 2.70[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P0AEP7 ) , eF-site , KEGG ( EC 4.1.1.47 ) , PISA