› 2ypr

X-ray diffraction
2.64Å resolution

Crystal structure of the DNA binding ETS domain of human protein FEV

Released:
DOI: 10.2210/pdb2ypr/pdb
PDB entry 2ypr coloured by chain, front view.
PDB entry 2ypr coloured by chain, side view.
PDB entry 2ypr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: DETERMINANTS OF DNA BINDING AND REDOX REGULATION BY DISULFIDE BOND FORMATION.
Cooper CD, Newman JA, Aitkenhead H, Allerston CK, Gileadi O
J Biol Chem 290 13692-709 (2015)
PMID: 25866208

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189226 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein FEV Chains: A, B
Molecule details ›
Chains: A, B
Length: 102 amino acids
Theoretical weight: 11.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99581 (Residues: 42-141; Coverage: 42%)
Gene names: FEV, PET1
Sequence domains: Ets-domain
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P4332
Unit cell:
a: 130.77Å b: 130.77Å c: 130.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.227
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Genetic-epigenetic interactions in cis: a major focus in the post-GWAS era.
Do et al. (2017)
2 more

3 mentions without citation

Recent advances in the structural molecular biology of Ets transcription factors: interactions, interfaces and inhibition.
Cooper et al. (2014)
2 more