X-ray diffraction
2.35Å resolution

Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese and L-malate


Function and Biology Details

Reaction catalysed:
Peptide L-aspartate + 2-oxoglutarate + O(2) = peptide 3-hydroxy-L-aspartate + succinate + CO(2)
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Aspartyl/asparaginyl beta-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 429 amino acids
Theoretical weight: 49.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q12797 (Residues: 330-758; Coverage: 57%)
Gene names: ASPH, BAH
Sequence domains:
Structure domains: B-lactam Antibiotic, Isopenicillin N Synthase; Chain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 49.019Å b: 70.641Å c: 172.541Å
α: 90° β: 90° γ: 90°
R R work R free
0.189 0.186 0.22
Expression system: Escherichia coli BL21(DE3)