5u7z

X-ray diffraction
2.5Å resolution

Human acid ceramidase (ASAH1, aCDase) self-activated

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for the activation of acid ceramidase.
Nat Commun 9 1621 (2018)
PMID: 29692406

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-171732 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Acid ceramidase subunit alpha Chains: A, C
Molecule details ›
Chains: A, C
Length: 129 amino acids
Theoretical weight: 14.87 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q13510 (Residues: 22-140; Coverage: 32%)
Gene names: ASAH, ASAH1, HSD-33, HSD33
Sequence domains: beta subunit of N-acylethanolamine-hydrolyzing acid amidase
Acid ceramidase subunit beta Chains: B, D
Molecule details ›
Chains: B, D
Length: 255 amino acids
Theoretical weight: 29.21 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q13510 (Residues: 141-395; Coverage: 68%)
Gene names: ASAH, ASAH1, HSD-33, HSD33
Sequence domains: Linear amide C-N hydrolases, choloylglycine hydrolase family

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2
Unit cell:
a: 153.667Å b: 68.312Å c: 97.805Å
α: 90° β: 120.72° γ: 90°
R-values:
R R work R free
0.235 0.234 0.271
Expression system: Spodoptera frugiperda