› 2wo4

X-ray diffraction
1.85Å resolution

3b' carbohydrate-binding module from the Cel9V glycoside hydrolase from Clostridium thermocellum, in-house data

Released:
DOI: 10.2210/pdb2wo4/pdb
PDB entry 2wo4 coloured by chain, front view.
PDB entry 2wo4 coloured by chain, side view.
PDB entry 2wo4 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Structure of a family 3b' carbohydrate-binding module from the Cel9V glycoside hydrolase from Clostridium thermocellum: structural diversity and implications for carbohydrate binding.
Petkun S, Jindou S, Shimon LJ, Rosenheck S, Bayer EA, Lamed R, Frolow F
Acta Crystallogr D Biol Crystallogr 66 33-43 (2010)
PMID: 20057047

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107076 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cellulase Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 18.65 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A3DJ30 (Residues: 731-888; Coverage: 17%)
Gene name: Cthe_2760
Sequence domains: Cellulose binding domain
Structure domains: Endoglucanase-like

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand SO4 1 x SO4
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P41212
Unit cell:
a: 73.897Å b: 73.897Å c: 85.755Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.148 0.191
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Molecular and biochemical analyses of CbCel9A/Cel48A, a highly secreted multi-modular cellulase by Caldicellulosiruptor bescii during growth on crystalline cellulose.
Yi et al. (2013)
6 more

1 mention without citation

AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis.
Schmelz et al. (2009)