› 1ia6

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF THE CELLULASE CEL9M OF C. CELLULOLYTICUM

Released:
DOI: 10.2210/pdb1ia6/pdb
PDB entry 1ia6 coloured by chain, front view.
PDB entry 1ia6 coloured by chain, side view.
PDB entry 1ia6 coloured by chain, top view.
Source organism: Ruminiclostridium cellulolyticum
Primary publication:
Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
Parsiegla G, Belaïch A, Belaïch JP, Haser R
Biochemistry 41 11134-42 (2002)
PMID: 12220178

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucanase Chain: A
Molecule details ›
Chain: A
Length: 441 amino acids
Theoretical weight: 48.7 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9EYQ2 (Residues: 31-471; Coverage: 89%)
Gene name: celM
Sequence domains: Glycosyl hydrolase family 9
Structure domains: Glycosyltransferase

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand ZN 1 x ZN
Ligand NI 1 x NI
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FU581
Spacegroup: P21
Unit cell:
a: 52.35Å b: 53.01Å c: 71.68Å
α: 90° β: 108.7° γ: 90°
R-values:
R R work R free
0.158 0.158 0.189
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Clostridium cellulolyticum: model organism of mesophilic cellulolytic clostridia.
Desvaux M. (2005)
4 more

5 mentions without citation

Cellulases: ambiguous nonhomologous enzymes in a genomic perspective.
Sukharnikov et al. (2011)
4 more