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› 7a1p

X-ray diffraction
1.76Å resolution

FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II), 4-propyl-2-oxoglutarate, AND CONSENSUS ANKYRIN REPEAT DOMAIN (20-MER)

Released:
DOI: 10.2210/pdb7a1p/pdb
Model geometry
Fit model/data
PDB entry 7a1p coloured by chain, front view.
PDB entry 7a1p coloured by chain, side view.
PDB entry 7a1p coloured by chain, top view.
Source organisms:
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
OpenAccess logo Nat Commun 12 6478 (2021)
PMID: 34759269

Function and Biology Details

Reactions catalysed: 
L-asparaginyl-[hypoxia-inducible factor alpha subunit] + 2-oxoglutarate +O2 = (3S)-3-hydroxy-L-asparaginyl-[hypoxia-inducible factor alphasubunit] + succinate + CO2.
(1) L-histidyl-[ankyrin-repeat domain protein] + 2-oxoglutarate + O2 =(3S)-3-hydroxy-L-histidyl-[ankyrin-repeat domain protein] + succinate +CO2.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-167974 (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
CONSENSUS ANKYRIN REPEAT DOMAIN Chain: B
Molecule details ›
Chain: B
Length: 20 amino acids
Theoretical weight: 2.17 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand SO4 3 x SO4
Ligand QW2 1 x QW2
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P41212
Unit cell:
a: 85.945Å b: 85.945Å c: 147.628Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.191
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

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