Cryo-EM structure of SKP1-FBXO22 in complex with a BACH1 BTB dimer at 3.2A resolution. Determined by electron microscopy at 3.2 Å resolution. Released 11 Dec 2024.
Explore 8S7D in 3D Show helices and sheets RCSB PDB PDBe
8S7D contains 33 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 | 7-8 | 2 | 1 |
| α-helix | 12-25 | 14 | |
| β-strand | 32-36 | 5 | 2 |
| β-strand | 39-43 | 5 | 2 |
| α-helix | 45-50 | 6 | |
| α-helix | 54-59 | 6 | |
| β-strand | 70 | 1 | 2 |
| α-helix | 77-89 | 13 | |
| β-strand | 91-94 | 4 | 3 |
| α-helix | 99-109 | 11 | |
| α-helix | 117-120 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 3 |
| α-helix | 12-26 | 15 | |
| β-strand | 32-36 | 5 | 4 |
| β-strand | 39-43 | 5 | 4 |
| α-helix | 45-51 | 7 | |
| β-strand | 52 | 1 | 5 |
| α-helix | 53-59 | 7 | |
| β-strand | 69-70 | 2 | 4 |
| α-helix | 77-89 | 13 | |
| β-strand | 91-92 | 2 | 1 |
| α-helix | 99-109 | 11 | |
| β-strand | 111 | 1 | 5 |
| α-helix | 116-122 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-22 | 4 | |
| α-helix | 27-31 | 5 | |
| α-helix | 54-63 | 10 | |
| α-helix | 87-92 | 6 | |
| α-helix | 97-110 | 14 | |
| α-helix | 113-127 | 15 | |
| α-helix | 132-139 | 8 | |
| α-helix | 141-143 | 3 | |
| α-helix | 147-156 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-25 | 7 | |
| α-helix | 27-35 | 9 | |
| α-helix | 39-45 | 7 | |
| α-helix | 50-61 | 12 | |
| β-strand | 67 | 1 | 6 |
| β-strand | 71 | 1 | 6 |
| α-helix | 84-91 | 8 | |
| β-strand | 99-107 | 9 | 6 |
| α-helix | 108-111 | 4 | |
| α-helix | 129-137 | 9 | |
| β-strand | 144-150 | 7 | 6 |
| β-strand | 153 | 1 | 7 |
| β-strand | 154-155 | 2 | 8 |
| α-helix | 164-165 | 2 | |
| β-strand | 166-167 | 2 | 8 |
| β-strand | 174-180 | 7 | 6 |
| β-strand | 191-193 | 3 | 9 |
| α-helix | 203-208 | 6 | |
| β-strand | 219-225 | 7 | 9 |
| α-helix | 236-243 | 8 | |
| β-strand | 249-255 | 7 | 9 |
| β-strand | 257-261 | 5 | 6 |
| β-strand | 274-280 | 7 | 9 |
| β-strand | 285 | 1 | 10 |
| β-strand | 287-288 | 2 | 3 |
| β-strand | 291 | 1 | 7 |
| α-helix | 299-310 | 12 | |
| β-strand | 319-326 | 8 | 7 |
| α-helix | 341-348 | 8 | |
| β-strand | 354-359 | 6 | 7 |
| β-strand | 362-363 | 2 | 9 |
| β-strand | 368-369 | 2 | 3 |
| β-strand | 373-378 | 6 | 3 |
| β-strand | 387-388 | 2 | 9 |
| β-strand | 393-398 | 6 | 7 |
| β-strand | 399 | 1 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription regulator protein BACH1 | A, B | protein | 125 | Homo sapiens | O14867 (AlphaFold model) |
| S-phase kinase-associated protein 1 | C | protein | 163 | Homo sapiens | P63208 (AlphaFold model) |
| F-box only protein 22 | D | protein | 395 | Homo sapiens | Q8NEZ5 (AlphaFold model) |
>8S7D_1 Transcription regulator protein BACH1 (chains A, B) QSMSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRI VGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCF QFLKF
>8S7D_2 S-phase kinase-associated protein 1 (chains C) MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQ WCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTC KTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
>8S7D_3 F-box only protein 22 (chains D) GGSGSSVDPRSTFVLSNLAEVVERVLTFLPAKALLRVACVCRLWRECVRRVLRTHRSVTW ISAGLAEAGHLEGHCLVRVVAEELENVRILPHTVLYMADSETFISLEECRGHKRARKRTS METALALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFPQIEGIKIQ PFHFIKDPKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLQQVVSTFSDMNI ILAGGQVDNLSSLTSEKNPLDIDASGVVGLSFSGHRIQSATVLLNEDVSDEKTAEAAMQR LKAANIPEHNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGNGEIGCDRI VTGNFILRKCNEVKDDDLFHSYTTIMALIHLGSSK
Dual BACH1 regulation by complementary SCF-type E3 ligases. Goretzki, B., Khoshouei, M., Schroder, M. et al. Cell (2024) 187:7585-7602.e25. DOI 10.1016/j.cell.2024.11.006 · PubMed
Other PDB entries of the same protein (UniProt O14867 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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