› 1ece

X-ray diffraction
2.4Å resolution

ACIDOTHERMUS CELLULOLYTICUS ENDOCELLULASE E1 CATALYTIC DOMAIN IN COMPLEX WITH A CELLOTETRAOSE

Released:
DOI: 10.2210/pdb1ece/pdb
PDB entry 1ece coloured by chain, front view.
PDB entry 1ece coloured by chain, side view.
PDB entry 1ece coloured by chain, top view.
Source organism: Acidothermus cellulolyticus
Primary publication:
Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose.
Sakon J, Adney WS, Himmel ME, Thomas SR, Karplus PA
Biochemistry 35 10648-60 (1996)
PMID: 8718854

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-157052 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endoglucanase E1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 40.26 KDa
Source organism: Acidothermus cellulolyticus
Expression system: Streptomyces lividans TK24
UniProt:
  • Canonical: P54583 (Residues: 42-399; Coverage: 69%)
Gene name: Acel_0614
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 97.13Å b: 97.13Å c: 258.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 0.236
Expression system: Streptomyces lividans TK24

Quick links

Citations

11 review citations

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

15 mentions without citation

Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
Garsoux et al. (2004)
14 more