› 3vog

X-ray diffraction
1.45Å resolution

Catalytic domain of the cellobiohydrolase, CcCel6A, from Coprinopsis cinerea

Released:
DOI: 10.2210/pdb3vog/pdb
Model geometry
Fit model/data
PDB entry 3vog coloured by chain, front view.
PDB entry 3vog coloured by chain, side view.
PDB entry 3vog coloured by chain, top view.
Source organism: Coprinopsis cinerea
Primary publication:
Comparison of the structural changes in two cellobiohydrolases, CcCel6A and CcCel6C, from Coprinopsis cinerea--a tweezer-like motion in the structure of CcCel6C.
Tamura M, Miyazaki T, Tanaka Y, Yoshida M, Nishikawa A, Tonozuka T
FEBS J 279 1871-82 (2012)
PMID: 22429290

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110642 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucanase Chain: A
Molecule details ›
Chain: A
Length: 373 amino acids
Theoretical weight: 41.05 KDa
Source organism: Coprinopsis cinerea
Expression system: Escherichia coli
UniProt:
  • Canonical: B7X9Z0 (Residues: 93-454; Coverage: 84%)
Gene name: CcCel6A
Sequence domains: Glycosyl hydrolases family 6
Structure domains: 1, 4-beta cellobiohydrolase

Ligands and Environments

1 bound ligand:
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 45.963Å b: 72.493Å c: 104.945Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.198
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center.
Ohnuma et al. (2014)
9 more

1 mention without citation

Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.
Tachioka et al. (2017)