PDBe 2gft

X-ray diffraction
2.3Å resolution

Crystal structure of the E263A nucleophile mutant of Bacillus licheniformis endo-beta-1,4-galactanase in complex with galactotriose

Released:
Source organism: Bacillus licheniformis
Entry authors: Welner D, Le Nours J, De Maria L, Jorgensen CT, Christensen LLH, Larsen S, Lo Leggio L

Function and Biology Details

Reaction catalysed:
The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arabinogalactan endo-beta-1,4-galactanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 399 amino acids
Theoretical weight: 43.72 KDa
Source organism: Bacillus licheniformis
Expression system: Bacillus subtilis
UniProt:
  • Canonical: Q65CX5 (Residues: 26-424; Coverage: 100%)
Gene names: BL00263, BLi04276, galA, ganB, yvfO
Sequence domains: Glycosyl hydrolase family 53
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 50.273Å b: 79.354Å c: 103.906Å
α: 90° β: 100.56° γ: 90°
R-values:
R R work R free
0.183 0.18 0.232
Expression system: Bacillus subtilis