2hbu

X-ray diffraction
1.85Å resolution

Crystal structure of HIF prolyl hydroxylase EGLN-1 in complex with a biologically active inhibitor

Released:
Source organism: Homo sapiens
Entry authors: Evdokimov AG, Walter RL, Mekel M, Pokross ME, Kawamoto R, Boyer A

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Egl nine homolog 1 Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 27.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9GZT9 (Residues: 188-426; Coverage: 56%)
Gene names: C1orf12, EGLN1, PNAS-118, PNAS-137
Sequence domains: 2OG-Fe(II) oxygenase superfamily
Structure domains: q2cbj1_9rhob like domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P63
Unit cell:
a: 111.045Å b: 111.045Å c: 40.126Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.231
Expression system: Escherichia coli