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1XIC

MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE

Summary for 1XIC
Entry DOI10.2210/pdb1xic/pdb
DescriptorD-XYLOSE ISOMERASE, D-xylose, MANGANESE (II) ION, ... (4 entities in total)
Functional Keywordsisomerase(intramolecular oxidoreductase)
Biological sourceStreptomyces rubiginosus
Cellular locationCytoplasm: P24300
Total number of polymer chains1
Total formula weight43514.24
Authors
Carrell, H.L.,Glusker, J.P. (deposition date: 1994-03-07, release date: 1994-06-22, Last modification date: 2024-02-14)
Primary citationCarrell, H.L.,Hoier, H.,Glusker, J.P.
Modes of binding substrates and their analogues to the enzyme D-xylose isomerase.
Acta Crystallogr.,Sect.D, 50:113-123, 1994
Cited by
PubMed Abstract: Studies of binding of substrates and inhibitors of the enzyme D-xylose isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that there are a variety of binding modes. These vary in the manner in which the substrate or its analogue extend, on binding, across the carboxy end of the (betaalpha)(8)-barrel structure. These binding sites are His54 and the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified in proposed mechanisms and their role in the binding of ligands is illustrated.
PubMed: 15299449
DOI: 10.1107/S0907444993009345
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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