› 2eqd

X-ray diffraction
2.8Å resolution

Crystal structure of Cel44A, GH family 44 endoglucanase from Clostridium thermocellum

Released:
DOI: 10.2210/pdb2eqd/pdb
PDB entry 2eqd coloured by chain, front view.
PDB entry 2eqd coloured by chain, side view.
PDB entry 2eqd coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum.
Kitago Y, Karita S, Watanabe N, Kamiya M, Aizawa T, Sakka K, Tanaka I
J Biol Chem 282 35703-11 (2007)
PMID: 17905739

Function and Biology Details

Reactions catalysed: 
Xyloglucan + H(2)O = xyloglucan oligosaccharides
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107038 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glycoside hydrolase family 9 Chain: A
Molecule details ›
Chain: A
Length: 519 amino acids
Theoretical weight: 57.69 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DD30 (Residues: 773-1287; Coverage: 33%)
Gene name: Cthe_0624
Sequence domains: Glycoside hydrolase family 44
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
4 bound ligands:
Ligand GOL 3 x GOL
Ligand ZN 1 x ZN
Ligand CA 1 x CA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 50.486Å b: 59.299Å c: 168.709Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.259
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Thermophilic lignocellulose deconstruction.
Blumer-Schuette et al. (2014)
18 other articles

2 mentions without citation

Vina-Carb: Improving Glycosidic Angles during Carbohydrate Docking.
Nivedha et al. (2016)
1 more