› 5oyc

X-ray diffraction
1.6Å 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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109886 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 5 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 396 amino acids
Theoretical weight: 44.4 KDa
Source organism: Cellvibrio japonicus Ueda107
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B3PD52 (Residues: 96-468; Coverage: 80%)
Gene names: CJA_3010, cel5D
Sequence domains: Cellulase (glycosyl hydrolase family 5)

Ligands and Environments

5 bound ligands:
Ligand GOL 20 x GOL
Ligand SO4 5 x SO4
Ligand PG4 2 x PG4
Ligand CL 1 x CL
Ligand 2PE 1 x 2PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 55.004Å b: 96.434Å c: 158.954Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.137 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy.
Glasgow et al. (2021)
10 other articles

1 mention without citation

A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis.
Glasgow et al. (2020)