8f9q

X-ray diffraction
2.76Å resolution

Guinea pig sialic acid esterase (SIAE)

Released:
Source organism: Cavia porcellus
Primary publication:
Structural Analysis of Mammalian Sialic Acid Esterase.
J Mol Biol 436 168801 (2024)
PMID: 39321866

Function and Biology Details

Reaction catalysed:
N-acetyl-O-acetylneuraminate + H(2)O = N-acetylneuraminate + acetate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-271278 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Sialate O-acetylesterase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 505 amino acids
Theoretical weight: 56.83 KDa
Source organism: Cavia porcellus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: H0VB40 (Residues: 24-518; Coverage: 100%)
Gene name: SIAE
Sequence domains: Carbohydrate esterase, sialic acid-specific acetylesterase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P64
Unit cell:
a: 206.554Å b: 206.554Å c: 155.19Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.204
Expression system: Spodoptera frugiperda