PDBe 1fob

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 100K

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arabinogalactan endo-beta-1,4-galactanase Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 36.78 KDa
Source organism: Aspergillus aculeatus
UniProt:
  • Canonical: P48842 (Residues: 17-350; Coverage: 100%)
Gene name: gal1
Sequence domains: Glycosyl hydrolase family 53
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: I222
Unit cell:
a: 59.7Å b: 87.98Å c: 128.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.251