PDBe 1pp4

X-ray diffraction
2.5Å resolution

The crystal structure of rhamnogalacturonan acetylesterase in space group P3121

Released:
Source organism: Aspergillus aculeatus
Primary publication:
Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase.
Acta Crystallogr. D Biol. Crystallogr. 60 472-8 (2004)
PMID: 14993671

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. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhamnogalacturonan acetylesterase Chains: A, B
Molecule details ›
Chains: A, B
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: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 75.36Å b: 75.36Å c: 212.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 0.222
Expression system: Aspergillus oryzae