X-ray diffraction
1.99Å resolution

Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and factor X substrate peptide fragment(39mer-4Ser)


Function and Biology Details

Reactions catalysed:
Peptide L-aspartate + 2-oxoglutarate + O(2) = peptide 3-hydroxy-L-aspartate + succinate + CO(2)
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
Factor X light chain Chain: B
Molecule details ›
Chain: B
Length: 39 amino acids
Theoretical weight: 4.19 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P00742 (Residues: 86-124; Coverage: 9%)
Gene name: F10
Sequence domains: EGF-like domain

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: 50.17Å b: 89.54Å c: 123.55Å
α: 90° β: 90° γ: 90°
R R work R free
0.192 0.191 0.205
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided