› 3abx

X-ray diffraction
1.4Å resolution

CcCel6C, a glycoside hydrolase family 6 enzyme, complexed with p-nitrophenyl beta-D-cellotrioside

Released:
DOI: 10.2210/pdb3abx/pdb
PDB entry 3abx coloured by chain, front view.
PDB entry 3abx coloured by chain, side view.
PDB entry 3abx coloured by chain, top view.
Source organism: Coprinopsis cinerea
Primary publication:
Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea.
Liu Y, Yoshida M, Kurakata Y, Miyazaki T, Igarashi K, Samejima M, Fukuda K, Nishikawa A, Tonozuka T
FEBS J 277 1532-42 (2010)
PMID: 20148970

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-110643 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucanase Chain: A
Molecule details ›
Chain: A
Length: 395 amino acids
Theoretical weight: 43.63 KDa
Source organism: Coprinopsis cinerea
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B7X9Z2 (Residues: 20-403; Coverage: 100%)
Gene name: CcCel6C
Sequence domains: Glycosyl hydrolases family 6
Structure domains: 1, 4-beta cellobiohydrolase

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand RCB 2 x RCB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P1
Unit cell:
a: 43.876Å b: 45.153Å c: 48.989Å
α: 77.63° β: 86.87° γ: 68.8°
R-values:
R R work R free
0.166 0.163 0.189
Expression system: Escherichia coli BL21(DE3)

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Citations

13 citation in other articles

Drechslerella stenobrocha genome illustrates the mechanism of constricting rings and the origin of nematode predation in fungi.
Liu et al. (2014)
12 more

1 mention without citation

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