The crystal structure of MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L in complex with H3K4me0 peptide. Determined by X-ray diffraction at 2.19 Å resolution. Released 7 Sept 2022.
Explore 7W67 in 3D Show helices and sheets RCSB PDB PDBe
7W67 contains 12 α-helices and 36 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 | 289-294 | 6 | 1 |
| β-strand | 299-300 | 2 | 2 |
| β-strand | 306-308 | 3 | 2 |
| β-strand | 314-318 | 5 | 1 |
| β-strand | 322 | 1 | 3 |
| β-strand | 325-335 | 11 | 2 |
| β-strand | 341-347 | 7 | 1 |
| β-strand | 363-367 | 5 | 1 |
| β-strand | 373-375 | 3 | 1 |
| β-strand | 378-380 | 3 | 1 |
| β-strand | 391-398 | 8 | 2 |
| β-strand | 446-451 | 6 | 2 |
| β-strand | 454-461 | 8 | 2 |
| α-helix | 463-465 | 3 | |
| β-strand | 468 | 1 | 3 |
| β-strand | 469-475 | 7 | 1 |
| β-strand | 479-483 | 5 | 2 |
| α-helix | 491-492 | 2 | |
| β-strand | 498-499 | 2 | 2 |
| α-helix | 500-503 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3816-3830 | 15 | |
| β-strand | 3831-3835 | 5 | 4 |
| β-strand | 3841-3845 | 5 | 4 |
| β-strand | 3849 | 1 | 5 |
| β-strand | 3854-3857 | 4 | 6 |
| β-strand | 3861-3864 | 4 | 7 |
| α-helix | 3865-3867 | 3 | |
| α-helix | 3868-3876 | 9 | |
| β-strand | 3885-3887 | 3 | 7 |
| β-strand | 3892-3895 | 4 | 7 |
| β-strand | 3899-3900 | 2 | 8 |
| α-helix | 3902-3905 | 4 | |
| α-helix | 3906 | 1 | |
| β-strand | 3907-3908 | 2 | 9 |
| β-strand | 3914-3921 | 8 | 6 |
| β-strand | 3924-3931 | 8 | 6 |
| β-strand | 3935 | 1 | 5 |
| α-helix | 3939 | 1 | |
| β-strand | 3940 | 1 | 4 |
| α-helix | 3941 | 1 | |
| β-strand | 3942-3943 | 2 | 9 |
| α-helix | 3947-3951 | 5 | |
| α-helix | 3952-3954 | 3 | |
| β-strand | 3957 | 1 | 10 |
| β-strand | 3968 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 337-338 | 2 | 8 |
| β-strand | 343-344 | 2 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Set1/Ash2 histone methyltransferase complex subunit ASH2 | A | protein | 184 | Homo sapiens | Q9UBL3 (AlphaFold model) |
| Histone-lysine N-methyltransferase 2A | C | protein | 158 | Homo sapiens | Q03164 |
| Retinoblastoma-binding protein 5 | F | protein | 27 | Homo sapiens | Q15291 (AlphaFold model) |
| Histone H3.3C | M | protein | 9 | Homo sapiens | Q6NXT2 (AlphaFold model) |
>7W67_1 Set1/Ash2 histone methyltransferase complex subunit ASH2 (chains A) SRVLLALHDRAPQLKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMPPDTAARL GWSQPLGNLQAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQGDVLGFYINLPEDTIS GRGSSEIIFYKNGVNQGVAYKDIFEGVYFPAISLYKSCTVSINFGPCFKYPPKDLTYRPM SDMG
>7W67_2 Histone-lysine N-methyltransferase 2A (chains C) DLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGIVIRSILTDKRE KYYDSKGIGSSYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAM RKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN
>7W67_3 Retinoblastoma-binding protein 5 (chains F) SAFAPDFKELDENVEYEERESEFDIED
>7W67_4 Histone H3.3C (chains M) ARTKQTARK
Structural basis for product specificities of MLL family methyltransferases. Li, Y., Zhao, L., Zhang, Y. et al. Mol Cell (2022) 82:3810-3825.e8. DOI 10.1016/j.molcel.2022.08.022 · PubMed
Other PDB entries of the same protein (UniProt Q9UBL3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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