1EDG

SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C

1EDG の概要

• エントリーDOI: 10.2210/pdb1edg/pdb
• 分子名称: ENDOGLUCANASE A (2 entities in total)
• 機能のキーワード: family a, cellulases, xylanases, family 5 of glycosyl hydrolase, cellulose degradation
• 由来する生物種: Clostridium cellulolyticum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43135.41

構造登録者

Ducros, V.,Czjzek, M.,Haser, R. (登録日: 1995-07-07, 公開日: 1996-08-17, 最終更新日: 2024-02-07)

主引用文献

Ducros, V.,Czjzek, M.,Belaich, A.,Gaudin, C.,Fierobe, H.P.,Belaich, J.P.,Davies, G.J.,Haser, R.
Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5.
Structure, 3:939-949, 1995

PubMed Abstract: Cellulases are glycosyl hydrolases--enzymes that hydrolyze glycosidic bonds. They have been widely studied using biochemical and microbiological techniques and have attracted industrial interest because of their potential in biomass conversion and in the paper and textile industries. Glycosyl hydrolases have lately been assigned to specific families on the basis of similarities in their amino acid sequences. The cellulase endoglucanase A produced by Clostridium cellulolyticum (CelCCA) belongs to family 5.

PubMed: 8535787
DOI: 10.1016/S0969-2126(01)00228-3

実験手法

X-RAY DIFFRACTION (1.6 Å)