› 6rk9

X-ray diffraction
2.29Å resolution

Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and cyclic peptide substrate mimic of factor X

Released:
DOI: 10.2210/pdb6rk9/pdb
PDB entry 6rk9 coloured by chain, front view.
PDB entry 6rk9 coloured by chain, side view.
PDB entry 6rk9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern.
Pfeffer I, Brewitz L, Krojer T, Jensen SA, Kochan GT, Kershaw NJ, Hewitson KS, McNeill LA, Kramer H, Münzel M, Hopkinson RJ, Oppermann U, Handford PA, McDonough MA, Schofield CJ
Nat Commun 10 4910 (2019)
PMID: 31659163

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

Assemblies composition:
hetero dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-167392 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartyl/asparaginyl beta-hydroxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 429 amino acids
Theoretical weight: 49.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q12797 (Residues: 330-758; Coverage: 57%)
Gene names: ASPH, BAH
Sequence domains:
Structure domains: B-lactam Antibiotic, Isopenicillin N Synthase; Chain
ACA-LYS-ASP-GLY-LEU-GLY-GLU-TYR-THR-CYS-THR-SER-LEU-GLU-GLY-PHE-GLU Chain: C
Molecule details ›
Chain: C
Length: 19 amino acids
Theoretical weight: 2.01 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand OGA 2 x OGA
1 modified residue:
Ligand DAL 1 x DAL

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P1
Unit cell:
a: 49.472Å b: 59.243Å c: 95.665Å
α: 103.97° β: 91.49° γ: 92.7°
R-values:
R R work R free
0.212 0.211 0.235
Expression systems:
  • Escherichia coli 'BL21-Gold(DE3)pLysS AG'
  • Not provided

Quick links

Citations

4 review citations

Aspartate β-hydroxylase as a target for cancer therapy.
Kanwal et al. (2020)
3 more