6dy0

X-ray diffraction
3.01Å resolution

Rabbit N-acylethanolamine-hydrolyzing acid amidase (NAAA) covalently bound to beta-lactam inhibitor ARN726, in presence of Triton X-100

Released:
Model geometry
Fit model/data
Source organism: Oryctolagus cuniculus
Primary publication:
Molecular mechanism of activation of the immunoregulatory amidase NAAA.
Proc Natl Acad Sci U S A 115 E10032-E10040 (2018)
PMID: 30301806

Function and Biology Details

Reactions catalysed:
N-acylsphingosine + H(2)O = a carboxylate + sphingosine
N-(long-chain-acyl)ethanolamine + H(2)O = a long-chain carboxylate + ethanolamine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-124215 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-acylethanolamine-hydrolyzing acid amidase subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 12.12 KDa
Source organism: Oryctolagus cuniculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: G1T7U7 (Residues: 31-47, 48-126; Coverage: 29%)
Gene name: NAAA
Sequence domains: beta subunit of N-acylethanolamine-hydrolyzing acid amidase
N-acylethanolamine-hydrolyzing acid amidase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 232 amino acids
Theoretical weight: 26.26 KDa
Source organism: Oryctolagus cuniculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: G1T7U7 (Residues: 127-358; Coverage: 70%)
Gene name: NAAA
Sequence domains: Linear amide C-N hydrolases, choloylglycine hydrolase family

Ligands and Environments

No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P4332
Unit cell:
a: 157.871Å b: 157.871Å c: 157.871Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.194 0.25
Expression system: Spodoptera frugiperda