The structure of the Suv4-20h2 ternary complex with histone H4. Determined by X-ray diffraction at 2.07 Å resolution. Released 22 May 2013.
Explore 4AU7 in 3D Show helices and sheets RCSB PDB PDBe
4AU7 contains 30 α-helices and 25 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 8-18 | 11 | |
| α-helix | 19-23 | 5 | |
| α-helix | 24-27 | 4 | |
| α-helix | 41-44 | 4 | |
| α-helix | 45-58 | 14 | |
| α-helix | 61-68 | 8 | |
| α-helix | 74-77 | 4 | |
| α-helix | 83-99 | 17 | |
| α-helix | 102-104 | 3 | |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 120-125 | 6 | 1 |
| β-strand | 129 | 1 | 2 |
| β-strand | 134-144 | 11 | 3 |
| α-helix | 147-152 | 6 | |
| β-strand | 162-165 | 4 | 3 |
| β-strand | 170-175 | 6 | 3 |
| α-helix | 177-180 | 4 | |
| α-helix | 181 | 1 | |
| β-strand | 182-183 | 2 | 3 |
| β-strand | 189-193 | 5 | 3 |
| β-strand | 198-203 | 6 | 3 |
| β-strand | 207 | 1 | 2 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 1 |
| α-helix | 213 | 1 | |
| β-strand | 214-215 | 2 | 3 |
| α-helix | 232-237 | 6 | |
| α-helix | 240-243 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-18 | 11 | |
| α-helix | 19-23 | 5 | |
| α-helix | 24-27 | 4 | |
| α-helix | 41-44 | 4 | |
| α-helix | 45-58 | 14 | |
| α-helix | 61-68 | 8 | |
| α-helix | 73-79 | 7 | |
| α-helix | 83-99 | 17 | |
| α-helix | 102-104 | 3 | |
| β-strand | 106-110 | 5 | 4 |
| β-strand | 121-125 | 5 | 4 |
| β-strand | 129 | 1 | 5 |
| β-strand | 134-144 | 11 | 6 |
| α-helix | 147-152 | 6 | |
| β-strand | 162-163 | 2 | 6 |
| β-strand | 172-175 | 4 | 6 |
| α-helix | 177-180 | 4 | |
| α-helix | 181 | 1 | |
| β-strand | 182-183 | 2 | 7 |
| β-strand | 189-193 | 5 | 6 |
| β-strand | 198-203 | 6 | 6 |
| β-strand | 207 | 1 | 5 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 4 |
| α-helix | 213 | 1 | |
| β-strand | 214-215 | 2 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20-22 | 3 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-lysine N-methyltransferase SUV420H2 | A, B | protein | 247 | MUS MUSCULUS | Q6Q783 (AlphaFold model) |
| Histone H4 peptide | C | protein | 9 | MUS MUSCULUS | P62806 (AlphaFold model) |
>4AU7_1 HISTONE-LYSINE N-METHYLTRANSFERASE SUV420H2 (chains A, B) SMGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPTLRRQHHLRSALEAFLRQR DLEAAFRALTLGGWMAHYFQSRAPRQEAALKTHIFCYLRAFLPESGFTILPCTRYSMETN GAKIVSTRAWKKNEKLELLVGCIAELREEDEDLLRAGENDFSIMYSTRKRSAQLWLGPAA FINHDCKPNCKFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGE GAFRLQP
>4AU7_2 HISTONE H4 PEPTIDE (chains C) RHRKVLRDY
Water and common crystallization additives (EDO) are not listed.
A Novel Route to Product Specificity in the Suv4-20 Family of Histone H4K20 Methyltransferases. Southall, S.M., Cronin, N.B., Wilson, J.R. Nucleic Acids Res (2014) 42:661. DOI 10.1093/NAR/GKT776 · PubMed
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