1XIH: Modes of Binding Substrates and Their Analogues to the Enzyme D-xylose Isomerase

Citation:
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.
PDB ID: 1XIHDownload
MMDB ID: 57691
PDB Deposition Date: 1994/3/7
Updated in MMDB: 2007/10 
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1XIH: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 1XIH
Label Count Molecule
Proteins (4 molecules)
4
D-xylose Isomerase
Molecule annotation
Chemicals (8 molecules)
1
4
2
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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