1edg

X-ray diffraction
1.6Å resolution

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

Released:

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase A Chain: A
Molecule details ›
Chain: A
Length: 380 amino acids
Theoretical weight: 43.14 KDa
Source organism: Ruminiclostridium cellulolyticum H10
Expression system: Escherichia coli
UniProt:
  • Canonical: P17901 (Residues: 27-401; Coverage: 84%)
Gene names: Ccel_1099, celCCA
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31, EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 52.4Å b: 76.2Å c: 113.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.22
Expression system: Escherichia coli