Cryo-EM structure of the human Sec61 complex inhibited by mycolactone. Determined by electron microscopy at 2.86 Å resolution. Released 24 May 2023.
Explore 8DO0 in 3D Show helices and sheets RCSB PDB PDBe
8DO0 contains 22 α-helices and 11 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 | 11-14 | 4 | |
| β-strand | 18-19 | 2 | 1 |
| α-helix | 20-21 | 2 | |
| α-helix | 28-46 | 19 | |
| β-strand | 49 | 1 | 2 |
| α-helix | 50 | 1 | |
| α-helix | 63-65 | 3 | |
| β-strand | 75 | 1 | 2 |
| α-helix | 82-97 | 16 | |
| α-helix | 108-133 | 26 | |
| α-helix | 140-170 | 31 | |
| α-helix | 178-196 | 19 | |
| β-strand | 200 | 1 | 3 |
| β-strand | 209 | 1 | 3 |
| α-helix | 212-222 | 11 | |
| α-helix | 226-234 | 9 | |
| α-helix | 242-259 | 18 | |
| β-strand | 262-268 | 7 | 4 |
| β-strand | 277-282 | 6 | 4 |
| α-helix | 289-311 | 23 | |
| α-helix | 316-321 | 6 | |
| β-strand | 323-324 | 2 | 5 |
| β-strand | 337-339 | 3 | 5 |
| α-helix | 351-356 | 6 | |
| α-helix | 358-382 | 25 | |
| α-helix | 387-397 | 11 | |
| β-strand | 400-401 | 2 | 4 |
| α-helix | 409-437 | 29 | |
| α-helix | 443-467 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-24 | 17 | |
| α-helix | 30-65 | 36 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 67-68 | 2 | 1 |
| α-helix | 70-95 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein transport protein Sec61 subunit gamma | B | protein | 68 | Homo sapiens | P60059 (AlphaFold model) |
| Protein transport protein Sec61 subunit beta | C | protein | 96 | Homo sapiens | P60468 (AlphaFold model) |
| Protein transport protein Sec61 subunit alpha isoform 1 | A | protein | 476 | Homo sapiens | P61619 (AlphaFold model) |
>8DO0_1 Protein transport protein Sec61 subunit gamma (chains B) MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIP INNIIVGG
>8DO0_2 Protein transport protein Sec61 subunit beta (chains C) MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYT EDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS
>8DO0_3 Protein transport protein Sec61 subunit alpha isoform 1 (chains A) MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSAD PFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFG MIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGIS LFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLP NLMNLIATIFVFAVVIYFQGFRYELPIRSTKVRGQIGIYPIKLFYTSNIPIILQSALVSN LYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCYYLSPPESFGSVLEDPVH AVVYIVFMLGSCAFFSKTWIEVSGSSPRDIAKQFKDQGMVINGKRETSIYRELKKIIPTA AAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF
| ID | Name | Formula | Copies |
|---|---|---|---|
| Q6B | [(6~{S},7~{S},9~{Z},12~{R})-12-[(~{Z},2~{S},6~{R},7~{R},9~{R})-4,6-dimethyl-7,9… | C44 H70 O9 | 1 |
A common mechanism of Sec61 translocon inhibition by small molecules. Itskanov, S., Wang, L., Junne, T. et al. Nat Chem Biol (2023) 19:1063-1071. DOI 10.1038/s41589-023-01337-y · PubMed
Other PDB entries of the same protein (UniProt P60059 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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