› 4zzv

X-ray diffraction
1.37Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucanase Chain: A
Molecule details ›
Chain: A
Length: 438 amino acids
Theoretical weight: 46.52 KDa
Source organism: Geotrichum candidum
UniProt:
  • Canonical: A0A088T0J9 (Residues: 18-455; Coverage: 85%)
Sequence domains: Glycosyl hydrolase family 7
Structure domains: Glycoside hydrolase, family 7, domain

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand NAG 2 x NAG
Ligand MAN 1 x MAN
Ligand MG 1 x MG
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 42.42Å b: 80.73Å c: 54.91Å
α: 90° β: 109.54° γ: 90°
R-values:
R R work R free
0.179 0.177 0.201

Quick links

Citations

2 review citations

Fungal cellulases: protein engineering and post-translational modifications.
Zhang et al. (2022)
1 more

1 mention without citation

Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C.
Borisova et al. (2015)