3qhn

X-ray diffraction
1.99Å resolution

Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii

Released:

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-129785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Glycoside hydrolase family 5 domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 458 amino acids
Theoretical weight: 51.92 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O58925 (Residues: 1-458; Coverage: 100%)
Gene name: PH1171
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: C2
Unit cell:
a: 162.325Å b: 58.347Å c: 138.271Å
α: 90° β: 109.61° γ: 90°
R-values:
R R work R free
0.198 0.196 0.248
Expression system: Escherichia coli