7p6j

X-ray diffraction
1.75Å resolution

Crystal structure of glycosyl-enzyme intermediate of RBcel1 Y201F

Released:
Source organism: uncultured bacterium
Entry authors: Collet L, Dutoit R

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
Macromolecules (6 distinct):
Cellulase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 321 amino acids
Theoretical weight: 36.37 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli MC1061
UniProt:
  • Canonical: C1JI15 (Residues: 31-351; Coverage: 100%)
Sequence domains: Cellulase (glycosyl hydrolase family 5)

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer : NEW Components: BGC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P21
Unit cell:
a: 88.56Å b: 90.54Å c: 89.68Å
α: 90° β: 118.77° γ: 90°
R-values:
R R work R free
0.174 0.172 0.202
Expression system: Escherichia coli MC1061