› 3oui

X-ray diffraction
1.7Å 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-190450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Egl nine homolog 1 Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 23.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9GZT9 (Residues: 181-392; Coverage: 50%)
Gene names: C1orf12, EGLN1, PNAS-118, PNAS-137
Sequence domains: 2OG-Fe(II) oxygenase superfamily
Structure domains: q2cbj1_9rhob like domain

Ligands and Environments

4 bound ligands:
Ligand ACT 2 x ACT
Ligand FE2 1 x FE2
Ligand 42Z 2 x 42Z
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 40.006Å b: 67.795Å c: 79.092Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.217
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Recent Advances in Developing Inhibitors for Hypoxia-Inducible Factor Prolyl Hydroxylases and Their Therapeutic Implications.
Kim et al. (2015)
3 more

3 mentions without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)
2 more