1k7c

X-ray diffraction
1.12Å resolution

Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution

Released:
Source organism: Aspergillus aculeatus
Primary publication:
A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase.
Acta Crystallogr D Biol Crystallogr 58 111-9 (2002)
PMID: 11752785

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, MAN
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 52.17Å b: 56.92Å c: 71.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.11 0.103 0.134
Expression system: Aspergillus oryzae