› 4eq1

X-ray diffraction
1.6Å resolution

Crystal Structure of the ARNT PAS-B homodimer

Released:
DOI: 10.2210/pdb4eq1/pdb
PDB entry 4eq1 coloured by chain, front view.
PDB entry 4eq1 coloured by chain, side view.
PDB entry 4eq1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulating the ARNT/TACC3 axis: multiple approaches to manipulating protein/protein interactions with small molecules.
Guo Y, Partch CL, Key J, Card PB, Pashkov V, Patel A, Bruick RK, Wurdak H, Gardner KH
ACS Chem Biol 8 626-35 (2013)
PMID: 23240775

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aryl hydrocarbon receptor nuclear translocator Chains: A, B
Molecule details ›
Chains: A, B
Length: 109 amino acids
Theoretical weight: 12.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P27540 (Residues: 357-464; Coverage: 14%)
Gene names: ARNT, BHLHE2
Sequence domains: PAS domain
Structure domains: PAS domain

Ligands and Environments

1 bound ligand:
Ligand PE5 1 x PE5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 93.315Å b: 61.678Å c: 55.514Å
α: 90° β: 124.6° γ: 90°
R-values:
R R work R free
0.203 0.202 0.226
Expression system: Escherichia coli

Quick links

Citations

5 review citations

bHLH-PAS proteins in cancer.
Bersten et al. (2013)
4 more

7 mentions without citation

bHLH-PAS Proteins: Their Structure and Intrinsic Disorder.
Kolonko et al. (2019)
6 more