› 4v0z

X-ray diffraction
1.7Å 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-158661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Exoglucanase 1 Chain: A
Molecule details ›
Chain: A
Length: 434 amino acids
Theoretical weight: 46.01 KDa
Source organism: Trichoderma reesei QM9414
UniProt:
  • Canonical: P62694 (Residues: 18-451; Coverage: 88%)
Gene name: cbh1
Sequence domains: Glycosyl hydrolase family 7
Structure domains: Glycoside hydrolase, family 7, domain

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
5 bound ligands:
Ligand NAG 1 x NAG
Ligand CO 2 x CO
Ligand GOL 1 x GOL
Ligand OPO 2 x OPO
Ligand PEG 1 x PEG
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: I222
Unit cell:
a: 83.063Å b: 81.375Å c: 109.942Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.13 0.129 0.157

Quick links

Citations

1 review citation

Mutexa: A Computational Ecosystem for Intelligent Protein Engineering.
Yang et al. (2023)
1 other article

1 mention without citation

Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non-productive binding: insights from crystal structures and MD simulation.
Haataja et al. (2023)