› 1h1n

X-ray diffraction
1.12Å resolution

Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus

Released:
DOI: 10.2210/pdb1h1n/pdb
PDB entry 1h1n coloured by chain, front view.
PDB entry 1h1n coloured by chain, side view.
PDB entry 1h1n coloured by chain, top view.
Source organism: Thermoascus aurantiacus
Primary publication:
Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus.
Van Petegem F, Vandenberghe I, Bhat MK, Van Beeumen J
Biochem Biophys Res Commun 296 161-6 (2002)
PMID: 12147244

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-186270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cellulase Chains: A, B
Molecule details ›
Chains: A, B
Length: 305 amino acids
Theoretical weight: 33.73 KDa
Source organism: Thermoascus aurantiacus
UniProt:
  • Canonical: Q8TG26 (Residues: 31-335; Coverage: 96%)
Gene name: eg1
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 75.764Å b: 84.728Å c: 89.099Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 not available 0.171

Quick links

Citations

8 citation in other articles

Function-based classification of carbohydrate-active enzymes by recognition of short, conserved peptide motifs.
Busk et al. (2013)
7 more

5 mentions without citation

3(10) helices in channels and other membrane proteins.
Vieira-Pires et al. (2010)
4 more