› 2rfw

X-ray diffraction
1.6Å resolution

Crystal Structure of Cellobiohydrolase from Melanocarpus albomyces

Released:
DOI: 10.2210/pdb2rfw/pdb
PDB entry 2rfw coloured by chain, front view.
PDB entry 2rfw coloured by chain, side view.
PDB entry 2rfw coloured by chain, top view.
Source organism: Melanocarpus albomyces
Primary publication:
Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding.
Parkkinen T, Koivula A, Vehmaanperä J, Rouvinen J
Protein Sci 17 1383-94 (2008)
PMID: 18499583

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-184982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucanase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 430 amino acids
Theoretical weight: 47.57 KDa
Source organism: Melanocarpus albomyces
Expression system: Trichoderma reesei
UniProt:
  • Canonical: Q8J0K6 (Residues: 23-452; Coverage: 100%)
Gene names: cel7B, gh7
Sequence domains: Glycosyl hydrolase family 7
Structure domains: Glycoside hydrolase, family 7, domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PCA 4 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P21
Unit cell:
a: 50.94Å b: 94.52Å c: 189.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 not available 0.243
Expression system: Trichoderma reesei

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Citations

4 review citations

Thermostable enzymes as biocatalysts in the biofuel industry.
Yeoman et al. (2010)
3 more

3 mentions without citation

Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding.
Parkkinen et al. (2008)
2 more