› 3h2w

X-ray diffraction
2.66Å resolution

Structure of A. acidocaldarius cellulase CelA in complex with cellobiose

Released:
DOI: 10.2210/pdb3h2w/pdb
PDB entry 3h2w coloured by chain, front view.
PDB entry 3h2w coloured by chain, side view.
PDB entry 3h2w coloured by chain, top view.
Source organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius
Primary publication:
Crystal structures of A. acidocaldarius endoglucanase Cel9A in complex with cello-oligosaccharides: strong -1 and -2 subsites mimic cellobiohydrolase activity.
Eckert K, Vigouroux A, Lo Leggio L, Moréra S
J Mol Biol 394 61-70 (2009)
PMID: 19729024

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
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
4 bound ligands:
Ligand BGC 1 x BGC
Ligand CA 1 x CA
Ligand ZN 1 x ZN
Ligand CO 2 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 84.892Å b: 129.398Å c: 48.965Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.254
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

Structural Basis for the Interconversion of Maltodextrins by MalQ, the Amylomaltase of Escherichia coli.
Weiss et al. (2015)