1dex

X-ray diffraction
1.9Å resolution

RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION

Released:

Function and Biology Details

Reaction catalysed:
Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-169387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Rhamnogalacturonan acetylesterase Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 24.62 KDa
Source organism: Aspergillus aculeatus
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: Q00017 (Residues: 18-250; Coverage: 100%)
Gene name: rha1
Sequence domains: GDSL-like Lipase/Acylhydrolase
Structure domains: SGNH hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 52.55Å b: 57.08Å c: 71.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 0.218
Expression system: Aspergillus oryzae