› 5v1b

X-ray diffraction
2.49Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188604 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl hydroxylase EGLN2 Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 26.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96KS0 (Residues: 167-403; Coverage: 58%)
Gene names: EGLN2, EIT6
Sequence domains: 2OG-Fe(II) oxygenase superfamily
Structure domains: q2cbj1_9rhob like domain

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand FE 1 x FE
Ligand 8UY 1 x 8UY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 66.717Å b: 112.082Å c: 66.223Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.236
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Structural Basis of Prolyl Hydroxylase Domain Inhibition by Molidustat.
Figg et al. (2021)
4 more

3 mentions without citation

The pyridazine heterocycle in molecular recognition and drug discovery.
Meanwell NA. (2023)
2 more