Cryo-EM Structure of FBOX22-BACH1BTB. Determined by electron microscopy at 3.8 Å resolution. Released 6 Nov 2024.
Explore 8UA3 in 3D Show helices and sheets RCSB PDB PDBe
8UA3 contains 21 α-helices and 42 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 |
|---|---|---|---|
| β-strand | 67-71 | 5 | 1 |
| α-helix | 73-75 | 3 | |
| α-helix | 83-91 | 9 | |
| α-helix | 92-94 | 3 | |
| β-strand | 101-106 | 6 | 1 |
| α-helix | 128-138 | 11 | |
| β-strand | 144-149 | 6 | 1 |
| β-strand | 153-155 | 3 | 2 |
| α-helix | 163-165 | 3 | |
| β-strand | 166-168 | 3 | 2 |
| β-strand | 174-179 | 6 | 1 |
| β-strand | 190-193 | 4 | 3 |
| α-helix | 205-208 | 4 | |
| β-strand | 217-220 | 4 | 4 |
| β-strand | 223-225 | 3 | 3 |
| α-helix | 232-243 | 12 | |
| β-strand | 249 | 1 | 4 |
| β-strand | 252 | 1 | 5 |
| β-strand | 254-255 | 2 | 3 |
| β-strand | 257-261 | 5 | 1 |
| α-helix | 267-269 | 3 | |
| β-strand | 274-277 | 4 | 3 |
| β-strand | 279-281 | 3 | 4 |
| β-strand | 286 | 1 | 6 |
| β-strand | 289 | 1 | 7 |
| β-strand | 291-292 | 2 | 2 |
| α-helix | 299-310 | 12 | |
| β-strand | 320-324 | 5 | 2 |
| β-strand | 325-326 | 2 | 8 |
| α-helix | 340-348 | 9 | |
| β-strand | 354-357 | 4 | 2 |
| β-strand | 358-359 | 2 | 8 |
| β-strand | 362-363 | 2 | 5 |
| β-strand | 367 | 1 | 7 |
| β-strand | 369 | 1 | 9 |
| β-strand | 373-374 | 2 | 9 |
| β-strand | 377 | 1 | 10 |
| β-strand | 387-388 | 2 | 5 |
| β-strand | 392-397 | 6 | 2 |
| β-strand | 398 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12 | 1 | 11 |
| α-helix | 16-29 | 14 | |
| β-strand | 36-40 | 5 | 12 |
| β-strand | 45-47 | 3 | 12 |
| α-helix | 49-55 | 7 | |
| α-helix | 70-71 | 2 | |
| β-strand | 72-75 | 4 | 12 |
| α-helix | 81-93 | 13 | |
| β-strand | 95 | 1 | 9 |
| β-strand | 98 | 1 | 10 |
| α-helix | 102-111 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9 | 1 | 10 |
| β-strand | 12-13 | 2 | 9 |
| α-helix | 16-28 | 13 | |
| β-strand | 36-40 | 5 | 13 |
| β-strand | 43-47 | 5 | 13 |
| α-helix | 52-55 | 4 | |
| α-helix | 58-63 | 6 | |
| α-helix | 67 | 1 | |
| β-strand | 72 | 1 | 13 |
| α-helix | 85-93 | 9 | |
| β-strand | 95 | 1 | 11 |
| α-helix | 103-113 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| F-box only protein 22 | C | protein | 403 | Homo sapiens | Q8NEZ5 (AlphaFold model) |
| Transcription regulator protein BACH1 | D, E | protein | 122 | Homo sapiens | O14867 (AlphaFold model) |
>8UA3_1 F-box only protein 22 (chains C) MEPVGCCGECRGSSVDPRSTFVLSNLAEVVERVLTFLPAKALLRVACVCRLWRECVRRVL RTHRSVTWISAGLAEAGHLEGHCLVRVVAEELENVRILPHTVLYMADSETFISLEECRGH KRARKRTSMETALALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFP QIEGIKIQPFHFIKDPKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLQQVV STFSDMNIILAGGQVDNLSSLTSEKNPLDIDASGVVGLSFSGHRIQSATVLLNEDVSDEK TAEAAMQRLKAANIPEHNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGN GEIGCDRIVTGNFILRKCNEVKDDDLFHSYTTIMALIHLGSSK
>8UA3_2 Transcription regulator protein BACH1 (chains D, E) SVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQ ADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFL KF
Recognition of BACH1 quaternary structure degrons by two F-box proteins under oxidative stress. Cao, S., Garcia, S.F., Shi, H. et al. Cell (2024) 187:7568-7584.e22. DOI 10.1016/j.cell.2024.10.012 · PubMed
Other PDB entries of the same protein (UniProt Q8NEZ5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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