5w78

X-ray diffraction
2.27Å resolution

Human acyloxyacyl hydrolase (AOAH), proteolytically processed

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of the mammalian lipopolysaccharide detoxifier.
Proc Natl Acad Sci U S A 115 E896-E905 (2018)
PMID: 29343645

Function and Biology Details

Reaction catalysed:
3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of bacterial toxin + a fatty acid
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-151164 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Acyloxyacyl hydrolase small subunit Chain: A
Molecule details ›
Chain: A
Length: 139 amino acids
Theoretical weight: 15.83 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P28039 (Residues: 24-152; Coverage: 23%)
Gene name: AOAH
Sequence domains: Saposin-like domain
Acyloxyacyl hydrolase large subunit Chain: B
Molecule details ›
Chain: B
Length: 423 amino acids
Theoretical weight: 48.19 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P28039 (Residues: 153-575; Coverage: 77%)
Gene name: AOAH
Sequence domains: GDSL-like Lipase/Acylhydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 50.402Å b: 87.356Å c: 146.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.201
Expression system: Spodoptera frugiperda