› 4b4f

X-ray diffraction
2.2Å resolution

Thermobifida fusca Cel6B(E3) co-crystallized with cellobiose

Released:
DOI: 10.2210/pdb4b4f/pdb
PDB entry 4b4f coloured by chain, front view.
PDB entry 4b4f coloured by chain, side view.
PDB entry 4b4f coloured by chain, top view.
Source organism: Thermobifida fusca
Primary publication:
The structure of a bacterial cellobiohydrolase: the catalytic core of the Thermobifida fusca family GH6 cellobiohydrolase Cel6B.
Sandgren M, Wu M, Karkehabadi S, Mitchinson C, Kelemen BR, Larenas EA, Ståhlberg J, Hansson H
J Mol Biol 425 622-35 (2013)
PMID: 23220193

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-178746 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Glucanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 45.47 KDa
Source organism: Thermobifida fusca
Expression system: Streptomyces lividans
UniProt:
  • Canonical: Q60029 (Residues: 177-596; Coverage: 75%)
Gene name: E3
Sequence domains: Glycosyl hydrolases family 6
Structure domains: 1, 4-beta cellobiohydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P21
Unit cell:
a: 42.95Å b: 106.7Å c: 92.47Å
α: 90° β: 89.96° γ: 90°
R-values:
R R work R free
0.189 0.186 0.244
Expression system: Streptomyces lividans

Quick links

Citations

1 review citation

Towards a molecular-level theory of carbohydrate processivity in glycoside hydrolases.
Beckham et al. (2014)
13 other articles

4 mentions without citation

Ligand-binding specificity and promiscuity of the main lignocellulolytic enzyme families as revealed by active-site architecture analysis.
Tian et al. (2016)
3 more