6yw4

X-ray diffraction
1.53Å resolution

HIF prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with N-oxalylglycine (NOG) and a RaPID-derived silent allosteric cyclic peptide 3C (14-mer)

Released:

Function and Biology Details

Reaction catalysed:
Hypoxia-inducible factor-L-proline + 2-oxoglutarate + O(2) = hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-167903 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Egl nine homolog 1 Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 25.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9GZT9 (Residues: 181-407; Coverage: 53%)
Gene names: C1orf12, EGLN1, PNAS-118, PNAS-137
Sequence domains: 2OG-Fe(II) oxygenase superfamily
PHD2-SPECIFIC RaPID CYCLIC PEPTIDE 3C (14-MER) Chain: B
Molecule details ›
Chain: B
Length: 14 amino acids
Theoretical weight: 1.8 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P65
Unit cell:
a: 46.622Å b: 46.622Å c: 203.711Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.162 0.177
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided