› 4b7e

X-ray diffraction
2.5Å resolution

FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH CONSENSUS ANKYRIN REPEAT DOMAIN-LEU PEPTIDE (20-MER)

Released:
DOI: 10.2210/pdb4b7e/pdb
PDB entry 4b7e coloured by chain, front view.
PDB entry 4b7e coloured by chain, side view.
PDB entry 4b7e coloured by chain, top view.
Source organisms:
Primary publication:
Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor.
Yang M, Hardy AP, Chowdhury R, Loik ND, Scotti JS, McCullagh JS, Claridge TD, McDonough MA, Ge W, Schofield CJ
Angew Chem Int Ed Engl 52 1700-4 (2013)
PMID: 23296631

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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164301 (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: Q9NWT6 (Residues: 1-349; Coverage: 100%)
Gene names: FIH1, HIF1AN
Sequence domains: Cupin-like domain
Structure domains:
CONSENSUS ANKYRIN REPEAT DOMAIN-LEU Chain: B
Molecule details ›
Chain: B
Length: 17 amino acids
Theoretical weight: 1.85 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand OGA 1 x OGA
Ligand SO4 5 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P41212
Unit cell:
a: 86.448Å b: 86.448Å c: 143.958Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.255
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

4 review citations

2-Oxoglutarate-Dependent Oxygenases.
Islam et al. (2018)
3 more

3 mentions without citation

Detection of peptide-binding sites on protein surfaces: the first step toward the modeling and targeting of peptide-mediated interactions.
Lavi et al. (2013)
2 more