3p6b

X-ray diffraction
2Å resolution

The crystal structure of CelK CBM4 from Clostridium thermocellum

Released:
Source organism: Acetivibrio thermocellus
Primary publication:
Structure of CBM4 from Clostridium thermocellum cellulase K.
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 527-30 (2011)
PMID: 21543854

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
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-143004 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellulose 1,4-beta-cellobiosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 205 amino acids
Theoretical weight: 23.58 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C2S1 (Residues: 27-210; Coverage: 21%)
Gene name: celK
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P41212
Unit cell:
a: 65.949Å b: 65.949Å c: 272.436Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.212 0.274
Expression system: Escherichia coli