› 7a1j

X-ray diffraction
1.9Å resolution

FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II) AND 3-(3-phenylpropyl)-2-oxoglutarate

Released:
DOI: 10.2210/pdb7a1j/pdb
PDB entry 7a1j coloured by chain, front view.
PDB entry 7a1j coloured by chain, side view.
PDB entry 7a1j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases.
Nakashima Y, Brewitz L, Tumber A, Salah E, Schofield CJ
Nat Commun 12 6478 (2021)
PMID: 34759269

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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: Q9NWT6 (Residues: 1-349; Coverage: 100%)
Gene names: FIH1, HIF1AN
Sequence domains: Cupin-like domain

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand SO4 5 x SO4
Ligand QVN 1 x QVN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P41212
Unit cell:
a: 86.194Å b: 86.194Å c: 148.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.209
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Combined proteomic and biochemical analyses redefine the consensus sequence requirement for epidermal growth factor-like domain hydroxylation.
Brewitz et al. (2022)
4 more