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X-ray diffraction
2.05Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartyl/asparaginyl beta-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 25.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12797 (Residues: 562-758; Coverage: 26%)
Gene names: ASPH, BAH
Sequence domains: Aspartyl/Asparaginyl beta-hydroxylase
Structure domains: B-lactam Antibiotic, Isopenicillin N Synthase; Chain

Ligands and Environments

3 bound ligands:
Ligand NI 1 x NI
Ligand LMR 1 x LMR
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3121
Unit cell:
a: 133.221Å b: 133.221Å c: 44.637Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.153 0.186
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Current Views on the Roles of O-Glycosylation in Controlling Notch-Ligand Interactions.
Saiki et al. (2021)
2 more

1 mention without citation

Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern.
Pfeffer et al. (2019)