3ndy

X-ray diffraction
2.1Å resolution

The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans

Released:
Source organism: Clostridium cellulovorans
Entry authors: Bianchetti CM, Smith RW, Bingman CA, Phillips Jr GN

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:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-541736 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Endoglucanase D Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 38.46 KDa
Source organism: Clostridium cellulovorans
Expression system: Escherichia coli
UniProt:
  • Canonical: P28623 (Residues: 32-376; Coverage: 71%)
Gene names: Clocel_3242, engD
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases
Endoglucanase D Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 107 amino acids
Theoretical weight: 11.12 KDa
Source organism: Clostridium cellulovorans
Expression system: Escherichia coli
UniProt:
  • Canonical: P28623 (Residues: 409-515; Coverage: 22%)
Gene names: Clocel_3242, engD
Sequence domains: Cellulose binding domain
Structure domains: Immunoglobulin-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 85.297Å b: 119.05Å c: 198.487Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.195
Expression system: Escherichia coli