5w7b

X-ray diffraction
1.9Å resolution

Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S262A mutant, with LPS

Released:
Source organism: Oryctolagus cuniculus
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-127586 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (6 distinct):
Acyloxyacyl hydrolase small subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 141 amino acids
Theoretical weight: 16.38 KDa
Source organism: Oryctolagus cuniculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O18823 (Residues: 23-153; Coverage: 23%)
Gene name: AOAH
Sequence domains: Saposin-like type B, region 2
Acyloxyacyl hydrolase large subunit Chains: C, D
Molecule details ›
Chains: C, D
Length: 422 amino acids
Theoretical weight: 47.62 KDa
Source organism: Oryctolagus cuniculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O18823 (Residues: 154-575; Coverage: 77%)
Gene name: AOAH
Sequence domains: GDSL-like Lipase/Acylhydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: PA1, GCS, KDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21212
Unit cell:
a: 109.522Å b: 138.806Å c: 89.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.213
Expression system: Spodoptera frugiperda