› 5jwp

X-ray diffraction
2.1Å resolution

Crystal structure of human FIH D201E variant in complex with Zn, alpha-ketoglutarate, and HIF1 alpha peptide.

Released:
DOI: 10.2210/pdb5jwp/pdb
PDB 5jwp coloured by chain and viewed from the front.
PDB 5jwp coloured by chain and viewed from the side.
PDB 5jwp coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
The facial triad in the ��-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to O2 activation.
Hangasky JA, Taabazuing CY, Martin CB, Eron SJ, Knapp MJ
J. Inorg. Biochem. 166 26-33 (2016)
PMID: 27815979

Function and Biology Details

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

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: 352 amino acids
Theoretical weight: 40.62 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
Structure domains:
Hypoxia-inducible factor 1-alpha Chain: B
Molecule details ›
Chain: B
Length: 19 amino acids
Theoretical weight: 2.02 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q16665 (Residues: 788-806; Coverage: 2%)
Gene names: BHLHE78, HIF1A, MOP1, PASD8
Sequence domains: HIF-1 alpha C terminal transactivation domain

Ligands and Environments

4 bound ligands:
Ligand AKG 1 x AKG
Ligand GOL 1 x GOL
Ligand ZN 1 x ZN
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P41212
Unit cell:
a: 86.22Å b: 86.22Å c: 149.903Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.17 0.209
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

1 review citation

Bridging angiogenesis and immune evasion in the hypoxic tumor microenvironment.
Schito L. (2018)
5 other articles

6 mentions without citation

The facial triad in the α-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to O2 activation.
Hangasky et al. (2017)
5 more