X-ray diffraction
3.05Å resolution

Crystal Structure of the CRTC2(SeMet)-CREB-CRE complex

Source organisms:
Primary publication:
Structural Insights into the CRTC2-CREB Complex Assembly on CRE.
J. Mol. Biol. 430 1926-1939 (2018)
PMID: 29733854

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct DNA molecule
Macromolecules (3 distinct):
Cyclic AMP-responsive element-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 59 amino acids
Theoretical weight: 7.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: P16220 (Residues: 269-327; Coverage: 18%)
Gene name: CREB1
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
CREB-regulated transcription coactivator 2 Chain: C
Molecule details ›
Chain: C
Length: 42 amino acids
Theoretical weight: 4.97 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
  • Canonical: Q3U182 (Residues: 17-58; Coverage: 6%)
Gene names: Crtc2, Torc2
Molecule details ›
Chain: B
Length: 20 nucleotides
Theoretical weight: 6.13 KDa

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: C2221
Unit cell:
a: 50.271Å b: 242.878Å c: 40.548Å
α: 90° β: 90° γ: 90°
R R work R free
0.232 0.228 0.269
Expression system: Escherichia coli BL21