PDBe 2his

X-ray diffraction
1.84Å resolution

CELLULOMONAS FIMI XYLANASE/CELLULASE DOUBLE MUTANT E127A/H205N WITH COVALENT CELLOBIOSE

Released:

Function and Biology Details

Reactions catalysed:
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exoglucanase/xylanase Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 33.97 KDa
Source organism: Cellulomonas fimi
Expression system: Escherichia coli
UniProt:
  • Canonical: P07986 (Residues: 42-353; Coverage: 70%)
Gene names: cex, xynB
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P41212
Unit cell:
a: 88.411Å b: 88.411Å c: 80.675Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.28
Expression system: Escherichia coli