› 1cem

X-ray diffraction
1.65Å resolution

ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395

Released:
DOI: 10.2210/pdb1cem/pdb
PDB entry 1cem coloured by chain, front view.
PDB entry 1cem coloured by chain, side view.
PDB entry 1cem coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum.
Alzari PM, Souchon H, Dominguez R
Structure 4 265-75 (1996)
PMID: 8805535

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-107021 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase A Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 40.35 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DC29 (Residues: 33-395; Coverage: 82%)
Gene names: Cthe_0269, celA
Sequence domains: Glycosyl hydrolases family 8
Structure domains: Glycosyltransferase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 50.118Å b: 63.518Å c: 104.974Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 0.191
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Microbial cellulose utilization: fundamentals and biotechnology.
Lynd et al. (2002)
11 more

15 mentions without citation

A graph-theory algorithm for rapid protein side-chain prediction.
Canutescu et al. (2003)
14 more