1XYM
THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID
Summary for 1XYM
Entry DOI | 10.2210/pdb1xym/pdb |
Descriptor | XYLOSE ISOMERASE, D-glucose, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | isomerase(intramolecular oxidoreductase) |
Biological source | Streptomyces olivochromogenes |
Total number of polymer chains | 2 |
Total formula weight | 86132.76 |
Authors | Allen, K.N.,Lavie, A.,Petsko, G.A.,Ringe, D. (deposition date: 1993-12-07, release date: 1994-05-31, Last modification date: 2024-02-14) |
Primary citation | Allen, K.N.,Lavie, A.,Glasfeld, A.,Tanada, T.N.,Gerrity, D.P.,Carlson, S.C.,Farber, G.K.,Petsko, G.A.,Ringe, D. Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid. Biochemistry, 33:1488-1494, 1994 Cited by PubMed: 7906142DOI: 10.1021/bi00172a027 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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