Cryo-EM structure of the human Sec61 complex inhibited by ipomoeassin F. Determined by electron microscopy at 3.01 Å resolution. Released 24 May 2023.
Explore 8DO1 in 3D Show helices and sheets RCSB PDB PDBe
8DO1 contains 27 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 | 5-13 | 9 | |
| β-strand | 18-19 | 2 | 1 |
| α-helix | 20-22 | 3 | |
| α-helix | 25-27 | 3 | |
| α-helix | 28-45 | 18 | |
| β-strand | 49 | 1 | 2 |
| α-helix | 50 | 1 | |
| α-helix | 59-60 | 2 | |
| β-strand | 75 | 1 | 2 |
| α-helix | 82-96 | 15 | |
| α-helix | 106-133 | 28 | |
| α-helix | 140-143 | 4 | |
| α-helix | 145-168 | 24 | |
| α-helix | 169-173 | 5 | |
| α-helix | 178-196 | 19 | |
| β-strand | 200 | 1 | 3 |
| β-strand | 209 | 1 | 3 |
| α-helix | 212-223 | 12 | |
| α-helix | 227-234 | 8 | |
| α-helix | 242-259 | 18 | |
| β-strand | 262-269 | 8 | 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 | 341-344 | 4 | |
| α-helix | 351-356 | 6 | |
| α-helix | 358-382 | 25 | |
| α-helix | 387-397 | 11 | |
| β-strand | 399-401 | 3 | 4 |
| α-helix | 410-414 | 5 | |
| α-helix | 417-438 | 22 | |
| 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 | 71-95 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein transport protein Sec61 subunit alpha isoform 1 | A | protein | 476 | Homo sapiens | P61619 (AlphaFold model) |
| 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) |
>8DO1_1 Protein transport protein Sec61 subunit alpha isoform 1 (chains A) MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSAD PFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFG MIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGIS LFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLP NLMNLIATIFVFAVVIYFQGFRYELPIRSTKVRGQIGIYPIKLFYTSNIPIILQSALVSN LYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCYYLSPPESFGSVLEDPVH AVVYIVFMLGSCAFFSKTWIEVSGSSPRDIAKQFKDQGMVINGKRETSIYRELKKIIPTA AAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF
>8DO1_2 Protein transport protein Sec61 subunit gamma (chains B) MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIP INNIIVGG
>8DO1_3 Protein transport protein Sec61 subunit beta (chains C) MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYT EDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS
| ID | Name | Formula | Copies |
|---|---|---|---|
| SXF | [(1~{S},3~{R},4~{S},5~{R},6~{R},8~{R},10~{S},23~{R},24~{R},25~{R},26~{R})-5-ace… | C44 H62 O15 | 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 P61619 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8DO1 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.