1XIG

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

1XIG の概要

• エントリーDOI: 10.2210/pdb1xig/pdb
• 分子名称: D-XYLOSE ISOMERASE, Xylitol, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: isomerase(intramolecular oxidoreductase)
• 由来する生物種: Streptomyces rubiginosus
• 細胞内の位置: Cytoplasm: P24300
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43516.26

構造登録者

Carrell, H.L.,Glusker, J.P. (登録日: 1994-03-07, 公開日: 1994-06-22, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)