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1XIB

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

7XIA」から置き換えられました2XIA」から置き換えられました
1XIB の概要
エントリーDOI10.2210/pdb1xib/pdb
分子名称D-XYLOSE ISOMERASE, MANGANESE (II) ION (3 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43364.11
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
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 1xib
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-27に公開中

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