1XIG

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

Summary for 1XIG

Entry DOI	10.2210/pdb1xig/pdb
Descriptor	D-XYLOSE ISOMERASE, Xylitol, MANGANESE (II) ION, ... (4 entities in total)
Functional Keywords	isomerase(intramolecular oxidoreductase)
Biological source	Streptomyces rubiginosus
Cellular location	Cytoplasm: P24300
Total number of polymer chains	1
Total formula weight	43516.26
Authors	Carrell, H.L.,Glusker, J.P. (deposition date: 1994-03-07, release date: 1994-06-22, Last modification date: 2024-02-14)
Primary citation	Carrell, 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 (1.7 Å)

Structure validation