Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH. Determined by X-ray diffraction at 1.75 Å resolution. Released 23 Nov 2004.
Explore 1XQH in 3D Show helices and sheets RCSB PDB PDBe
1XQH contains 16 α-helices and 42 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 | 118-122 | 5 | 1 |
| β-strand | 128-132 | 5 | 1 |
| β-strand | 141-147 | 7 | 1 |
| β-strand | 153-160 | 8 | 1 |
| β-strand | 163-176 | 14 | 1 |
| β-strand | 179-184 | 6 | 1 |
| α-helix | 185 | 1 | |
| β-strand | 190-191 | 2 | 1 |
| α-helix | 210-213 | 4 | |
| β-strand | 216-220 | 5 | 2 |
| β-strand | 228-232 | 5 | 2 |
| β-strand | 236 | 1 | 3 |
| β-strand | 241-245 | 5 | 4 |
| β-strand | 248-250 | 3 | 5 |
| α-helix | 252-257 | 6 | |
| α-helix | 260-262 | 3 | |
| β-strand | 267-268 | 2 | 5 |
| β-strand | 274-276 | 3 | 5 |
| α-helix | 292-294 | 3 | |
| α-helix | 295 | 1 | |
| β-strand | 296-297 | 2 | 4 |
| β-strand | 303-310 | 8 | 4 |
| β-strand | 314-321 | 8 | 4 |
| β-strand | 325 | 1 | 3 |
| α-helix | 329 | 1 | |
| β-strand | 330-331 | 2 | 2 |
| β-strand | 332-333 | 2 | 4 |
| α-helix | 351-361 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 372 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 118-122 | 5 | 1 |
| β-strand | 128-132 | 5 | 1 |
| β-strand | 141-147 | 7 | 1 |
| β-strand | 153-160 | 8 | 1 |
| β-strand | 163-176 | 14 | 1 |
| β-strand | 179-184 | 6 | 1 |
| α-helix | 185 | 1 | |
| β-strand | 190-191 | 2 | 1 |
| α-helix | 210-213 | 4 | |
| β-strand | 216-220 | 5 | 6 |
| β-strand | 228-232 | 5 | 6 |
| β-strand | 236 | 1 | 7 |
| β-strand | 241-245 | 5 | 8 |
| β-strand | 248-250 | 3 | 9 |
| α-helix | 252-256 | 5 | |
| α-helix | 260-262 | 3 | |
| β-strand | 267-268 | 2 | 9 |
| β-strand | 274-276 | 3 | 9 |
| α-helix | 292-294 | 3 | |
| α-helix | 295 | 1 | |
| β-strand | 296-297 | 2 | 8 |
| β-strand | 303-310 | 8 | 8 |
| β-strand | 314-321 | 8 | 8 |
| β-strand | 325 | 1 | 7 |
| α-helix | 329 | 1 | |
| β-strand | 330-331 | 2 | 6 |
| β-strand | 332-333 | 2 | 8 |
| α-helix | 351-360 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-lysine N-methyltransferase, H3 lysine-4 specific | A, E | protein | 264 | Homo sapiens | Q8WTS6 (AlphaFold model) |
| 9-mer peptide from tumor protein p53 | B, F | protein | 10 | P04637 (AlphaFold model) |
>1XQH_1 Histone-lysine N-methyltransferase, H3 lysine-4 specific (chains A, E) GPLGSGQYKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDG EMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESL ISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYN HVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPP GKSGPEAPEWYQVELKAFQATQQK
>1XQH_2 9-mer peptide from tumor protein p53 (chains B, F) LKSKKGQSTY
| ID | Name | Formula | Copies |
|---|---|---|---|
| SAH | S-adenosyl-L-homocysteine | C14 H20 N6 O5 S | 2 |
Regulation of p53 activity through lysine methylation. Chuikov, S., Kurash, J.K., Wilson, J.R. et al. Nature (2004) 432:353-360. DOI 10.1038/nature03117 · PubMed
Other PDB entries of the same protein (UniProt Q8WTS6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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