› 1md0

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1

Released:
DOI: 10.2210/pdb1md0/pdb
PDB entry 1md0 coloured by chain, front view.
PDB entry 1md0 coloured by chain, side view.
PDB entry 1md0 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships.
Garvie CW, Pufall MA, Graves BJ, Wolberger C
J Biol Chem 277 45529-36 (2002)
PMID: 12221090

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151031 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein C-ets-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 141 amino acids
Theoretical weight: 16.37 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27577 (Residues: 300-440; Coverage: 32%)
Gene names: Ets-1, Ets1
Sequence domains: Ets-domain
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 53.35Å b: 66.67Å c: 83.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Genomic and biochemical insights into the specificity of ETS transcription factors.
Hollenhorst et al. (2011)
9 more

3 mentions without citation

Structured and disordered regions cooperatively mediate DNA-binding autoinhibition of ETS factors ETV1, ETV4 and ETV5.
Currie et al. (2017)
2 more