1EDG

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

Summary for 1EDG

• Entry DOI: 10.2210/pdb1edg/pdb
• Descriptor: ENDOGLUCANASE A (2 entities in total)
• Functional Keywords: family a, cellulases, xylanases, family 5 of glycosyl hydrolase, cellulose degradation
• Biological source: Clostridium cellulolyticum
• Total number of polymer chains: 1
• Total formula weight: 43135.41

Authors

Ducros, V.,Czjzek, M.,Haser, R. (deposition date: 1995-07-07, release date: 1996-08-17, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)