1XYL

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 1XYL

Entry DOI	10.2210/pdb1xyl/pdb
Descriptor	XYLOSE ISOMERASE, MAGNESIUM ION, HYDROXIDE ION, ... (4 entities in total)
Functional Keywords	isomerase(intramolecular oxidoreductase)
Biological source	Streptomyces olivochromogenes
Cellular location	Cytoplasm: P15587
Total number of polymer chains	2
Total formula weight	85772.45
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: 7906142 DOI: 10.1021/bi00172a027 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation