› 7jsa

X-ray diffraction
2.85Å resolution

Crystal structure of the DNA binding domain of human transcription factor ERF in the reduced form, in complex with double-stranded DNA ACCGGAAGTG

Released:
DOI: 10.2210/pdb7jsa/pdb
PDB entry 7jsa coloured by chain, front view.
PDB entry 7jsa coloured by chain, side view.
PDB entry 7jsa coloured by chain, top view.
Source organisms:
Primary publication:
Structural Insight into the DNA Binding Function of Transcription Factor ERF.
Hou C, McCown C, Ivanov DN, Tsodikov OV
Biochemistry (2020)
PMID: 33175491

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-121397 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
ETS domain-containing transcription factor ERF Chain: J
Molecule details ›
Chain: J
Length: 123 amino acids
Theoretical weight: 14.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P50548 (Residues: 22-140; Coverage: 22%)
Gene name: ERF
Sequence domains: Ets-domain
DNA (5'-D(*AP*CP*CP*GP*GP*AP*AP*GP*TP*G)-3') Chain: B
Molecule details ›
Chain: B
Length: 10 nucleotides
Theoretical weight: 3.09 KDa
Source organism: synthetic construct
Expression system: Not provided
DNA (5'-D(*CP*AP*CP*TP*TP*CP*CP*GP*GP*T)-3') Chain: C
Molecule details ›
Chain: C
Length: 10 nucleotides
Theoretical weight: 3 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P41212
Unit cell:
a: 63.798Å b: 63.798Å c: 137.502Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.247 0.275
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

1 citations in other articles

The CIC-ERF co-deletion underlies fusion-independent activation of ETS family member, ETV1, to drive prostate cancer progression.
Gupta et al. (2022)

1 mention without citation

Structural Insight into the DNA Binding Function of Transcription Factor ERF.
Hou et al. (2020)