Seminal Fluid Protein PDC-109 (Domain B)
A common protein fold and similar active site in two distinct families of beta-glycanases.
X-ray crystallography (1.64 Angstroms) of 27-406
Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5.
Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose.
X-ray crystallography (2.3 Angstroms) of mutant GLN-140.
The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism.
Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi.
X-ray crystallography (1.57 Angstroms) of 30-329
Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution.
X-ray crystallography (1.64 Angstroms) of 30-329
Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase.
X-ray crystallography (1.75/1.95/2.1 Angstroms)
Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form.
X-ray crystallography (2.3 Angstroms) of 44-335
Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi.
A novel combination of two classic catalytic schemes.
This family belongs to glycosidase family-5, which has an retaining mechanism (equatorial to equatorial conformation), and also a family of 4/7 superfamily, which has got catalytic residues at the C-terminal ends of beta-4 and beta-7 on the (alpha/beta)8 barrel fold. This enzyme is composed of the N-terminal catalytic domain and the C-terminal Cellulose-binding domain. The structure of the C-terminal domain has not been determined yet. This enzyme must have the same catalytic mechanism as that of the other TIM barrel cellulases (S00203, D00502 & D00503 in EzCatDB).