PDBe 1h2l

X-ray diffraction
2.25Å resolution

Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide

Released:

Function and Biology Details

Reactions catalysed:
Hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O(2) = hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO(2)
[Ankyrin-repeat domain protein]-L-asparagine + 2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-hydroxy-L-asparagine + succinate + CO(2) 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hypoxia-inducible factor 1-alpha inhibitor Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 40.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW Q9NWT6 (Residues: 1-349; Coverage: 100%)
Gene names: FIH1, HIF1AN
Sequence domains: Cupin-like domain
Structure domains:
Hypoxia-inducible factor 1-alpha Chain: S
Molecule details ›
Chain: S
Length: 41 amino acids
Theoretical weight: 4.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW Q16665 (Residues: 786-826; Coverage: 5%)
Gene names: BHLHE78, HIF1A, MOP1, PASD8
Sequence domains: HIF-1 alpha C terminal transactivation domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P41212
Unit cell:
a: 86.264Å b: 86.264Å c: 147.914Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.217
Expression system: Escherichia coli BL21(DE3)