The crystal structure of MLL1 (N3861I/Q3867L) in complex with RbBP5 and Ash2L. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Feb 2016.
Explore 5F6L in 3D Show helices and sheets RCSB PDB PDBe
5F6L contains 12 α-helices and 35 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 | 3816-3830 | 15 | |
| β-strand | 3831-3835 | 5 | 6 |
| β-strand | 3841-3845 | 5 | 6 |
| β-strand | 3849 | 1 | 7 |
| β-strand | 3854-3857 | 4 | 8 |
| β-strand | 3861-3864 | 4 | 2 |
| α-helix | 3865-3867 | 3 | |
| α-helix | 3868-3878 | 11 | |
| α-helix | 3880-3882 | 3 | |
| β-strand | 3884-3886 | 3 | 2 |
| β-strand | 3891-3894 | 4 | 2 |
| β-strand | 3898-3899 | 2 | 1 |
| α-helix | 3901-3904 | 4 | |
| α-helix | 3905 | 1 | |
| β-strand | 3906-3907 | 2 | 9 |
| β-strand | 3913-3920 | 8 | 8 |
| β-strand | 3923-3930 | 8 | 8 |
| β-strand | 3934 | 1 | 7 |
| α-helix | 3938 | 1 | |
| β-strand | 3939 | 1 | 6 |
| α-helix | 3940 | 1 | |
| β-strand | 3941-3942 | 2 | 9 |
| α-helix | 3946-3948 | 3 | |
| β-strand | 3956 | 1 | 10 |
| β-strand | 3967 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 289-294 | 6 | 3 |
| β-strand | 299-300 | 2 | 4 |
| β-strand | 306-308 | 3 | 4 |
| β-strand | 314-318 | 5 | 3 |
| β-strand | 322 | 1 | 5 |
| β-strand | 325-335 | 11 | 4 |
| β-strand | 341-347 | 7 | 3 |
| β-strand | 363-367 | 5 | 3 |
| β-strand | 373-375 | 3 | 3 |
| β-strand | 378-380 | 3 | 3 |
| β-strand | 391-398 | 8 | 4 |
| β-strand | 446-451 | 6 | 4 |
| β-strand | 454-461 | 8 | 4 |
| α-helix | 463-464 | 2 | |
| β-strand | 468 | 1 | 5 |
| β-strand | 469-475 | 7 | 3 |
| β-strand | 479-483 | 5 | 4 |
| α-helix | 491-492 | 2 | |
| β-strand | 498-499 | 2 | 4 |
| α-helix | 500-503 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 337-338 | 2 | 1 |
| β-strand | 343-344 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoblastoma-binding protein 5 | J | protein | 27 | Homo sapiens | Q15291 (AlphaFold model) |
| Set1/Ash2 histone methyltransferase complex subunit ASH2 | B | protein | 184 | Homo sapiens | Q9UBL3 (AlphaFold model) |
| Histone-lysine N-methyltransferase 2A | A | protein | 158 | Homo sapiens | Q03164 |
>5F6L_1 Retinoblastoma-binding protein 5 (chains J) SAFAPDFKELDENVEYEERESEFDIED
>5F6L_2 Set1/Ash2 histone methyltransferase complex subunit ASH2 (chains B) SRVLLALHDRAPQLKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMPPDTAARL GWSQPLGNLQAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQGDVLGFYINLPEDTIS GRGSSEIIFYKNGVNQGVAYKDIFEGVYFPAISLYKSCTVSINFGPCFKYPPKDLTYRPM SDMG
>5F6L_3 Histone-lysine N-methyltransferase 2A (chains A) SDLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGIVIRSILTDKR EKYYDSKGIGCYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAM RKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN
Structural basis for activity regulation of MLL family methyltransferases. Li, Y., Han, J., Zhang, Y. et al. Nature (2016) 530:447-452. DOI 10.1038/nature16952 · PubMed
Other PDB entries of the same protein (UniProt Q15291 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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