1XIB

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

Replaces:  7XIAReplaces:  2XIA

Summary for 1XIB

• Entry DOI: 10.2210/pdb1xib/pdb
• Descriptor: D-XYLOSE ISOMERASE, MANGANESE (II) ION (3 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: 43364.11

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

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)