5vjx

X-ray diffraction
2.7Å resolution

Crystal structure of the CLOCK Transcription Domain Exon19 in Complex with a Repressor

Released:
Source organism: Mus musculus

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-126673 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CLOCK-interacting pacemaker Chains: A, D, G, J, M, R, U, X, a, d
Molecule details ›
Chains: A, D, G, J, M, R, U, X, a, d
Length: 64 amino acids
Theoretical weight: 7.21 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8R0W1 (Residues: 352-414; Coverage: 15%)
Gene names: Cipc, Kiaa1737
Circadian locomoter output cycles protein kaput Chains: B, C, E, F, H, I, K, L, N, O, S, T, V, W, Y, Z, b, c, e, f
Molecule details ›
Chains: B, C, E, F, H, I, K, L, N, O, S, T, V, W, Y, Z, b, c, e, f
Length: 51 amino acids
Theoretical weight: 6.2 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O08785 (Residues: 515-560; Coverage: 5%)
Gene name: Clock

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 175.536Å b: 116.836Å c: 132.926Å
α: 90° β: 126.54° γ: 90°
R-values:
R R work R free
0.221 0.218 0.275
Expression system: Escherichia coli