Crystal structure of Oxpecker chromodomain in complex with H3K9me3. Determined by X-ray diffraction at 1.7 Å resolution. Released 26 Oct 2022.
Explore 7VRF in 3D Show helices and sheets RCSB PDB PDBe
7VRF contains 8 α-helices and 10 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 21-23 | 3 | 1 |
| β-strand | 24-33 | 10 | 2 |
| β-strand | 36-43 | 8 | 2 |
| α-helix | 48-50 | 3 | |
| β-strand | 52-55 | 4 | 2 |
| α-helix | 56-58 | 3 | |
| α-helix | 60-62 | 3 | |
| α-helix | 63-78 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 21-23 | 3 | 3 |
| β-strand | 24-33 | 10 | 4 |
| β-strand | 36-43 | 8 | 4 |
| α-helix | 48-50 | 3 | |
| β-strand | 52-55 | 4 | 4 |
| α-helix | 56-58 | 3 | |
| α-helix | 60-62 | 3 | |
| α-helix | 63-76 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-8 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Oxpecker | A, B | protein | 71 | Drosophila melanogaster | A1ZAW9 (AlphaFold model) |
| H3K9me3 | C, D | protein | 11 | Drosophila melanogaster | P02299 (AlphaFold model) |
>7VRF_1 Oxpecker (chains A, B) NVKEKSSEYIVEKFLGKRYLRGRPQYLTKWEGYPIEQCTWEPLENLGKCMTLIADYEAEL FQQSREKKNDQ
>7VRF_2 H3K9me3 (chains C, D) KQTARKSTGGK
Structural insights into the chromodomain of Oxpecker in complex with histone H3 lysine 9 trimethylation reveal a transposon silencing mechanism by heterodimerization. Jin, Z., Yu, B., Huang, Y. Biochem Biophys Res Commun (2023) 652:95-102. DOI 10.1016/j.bbrc.2023.02.045 · PubMed
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