› 3gzk

X-ray diffraction
1.8Å resolution

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-189570 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase Chain: A
Molecule details ›
Chain: A
Length: 537 amino acids
Theoretical weight: 59.03 KDa
Source organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9AJS0 (Residues: 1-537; Coverage: 100%)
Gene name: celA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand ZN 1 x ZN
Ligand MPD 2 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 84.92Å b: 129.3Å c: 49.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.213
Expression system: Escherichia coli

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Citations

1 review citation

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

6 mentions without citation

Thermostability in endoglucanases is fold-specific.
Yennamalli et al. (2011)
5 more