4u68

X-ray diffraction
1.8Å resolution

Crystal structure of Rhino chromodomain in complex with H3K9me3

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chromo domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 75 amino acids
Theoretical weight: 8.44 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7JXA8 (Residues: 20-90; Coverage: 17%)
Gene names: CG10683, Dmel\CG10683, Dmel_CG10683, HP1, HP1D, HP1d, RHI, Rhi, Rhino, hp1d, rhi, rhino, rno
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Histone H3.1 Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 11 amino acids
Theoretical weight: 1.21 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 5-15; Coverage: 8%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 50.946Å b: 67.679Å c: 79.75Å
α: 90° β: 106.46° γ: 90°
R-values:
R R work R free
0.186 0.184 0.206
Expression systems:
  • Escherichia coli
  • Not provided