› 1fce

X-ray diffraction
2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153468 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endoglucanase F Chain: A
Molecule details ›
Chain: A
Length: 629 amino acids
Theoretical weight: 70.87 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37698 (Residues: 30-658; Coverage: 91%)
Gene names: Ccel_0729, celCCF
Sequence domains: Glycosyl hydrolase family 48
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: MGL, SGC, BGC
Ligand MGL 2 x MGL
Ligand SGC 2 x SGC
Ligand BGC 4 x BGC
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 61.45Å b: 84.54Å c: 121.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.165 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Microbial cellulose utilization: fundamentals and biotechnology.
Lynd et al. (2002)
12 more

4 mentions without citation

Conformational diversity analysis reveals three functional mechanisms in proteins.
Monzon et al. (2017)
3 more