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Structure paper

TitleRole 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.
Journal, issue, pagesBiochemistry, Vol. 33, Page 1488-1494, Year 1994
Publish dateDec 7, 1993 (structure data deposition date)
AuthorsAllen, K.N. / Lavie, A. / Glasfeld, A. / Tanada, T.N. / Gerrity, D.P. / Carlson, S.C. / Farber, G.K. / Petsko, G.A. / Ringe, D.
External linksBiochemistry / PubMed:7906142
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-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
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-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
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-OH:
HYDROXIDE ION

ChemComp-HOH:
WATER

ChemComp-GLO:
D-glucose

Source
  • streptomyces olivochromogenes (bacteria)
KeywordsISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)

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