Cryo-EM structure of the human Sec61 complex in a partially-open apo state (Class 1). Determined by electron microscopy at 3.03 Å resolution. Released 24 May 2023.
Explore 8DNV in 3D Show helices and sheets RCSB PDB PDBe
8DNV contains 26 α-helices and 13 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 | 10-14 | 5 | |
| 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 | |
| β-strand | 55 | 1 | 3 |
| α-helix | 59-60 | 2 | |
| α-helix | 66-69 | 4 | |
| β-strand | 75 | 1 | 2 |
| α-helix | 82-97 | 16 | |
| α-helix | 110-132 | 23 | |
| β-strand | 137 | 1 | 3 |
| α-helix | 140-143 | 4 | |
| α-helix | 146-171 | 26 | |
| α-helix | 178-196 | 19 | |
| β-strand | 200-202 | 3 | 4 |
| β-strand | 207-209 | 3 | 4 |
| α-helix | 212-222 | 11 | |
| α-helix | 227-234 | 8 | |
| α-helix | 242-259 | 18 | |
| β-strand | 262-269 | 8 | 5 |
| β-strand | 277-282 | 6 | 5 |
| α-helix | 289-311 | 23 | |
| α-helix | 316-321 | 6 | |
| β-strand | 323-324 | 2 | 6 |
| β-strand | 337-339 | 3 | 6 |
| 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 | 5 |
| α-helix | 410-438 | 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 | 70-94 | 25 |
| 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) |
>8DNV_1 Protein transport protein Sec61 subunit gamma (chains B) MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIP INNIIVGG
>8DNV_2 Protein transport protein Sec61 subunit beta (chains C) MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYT EDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS
>8DNV_3 Protein transport protein Sec61 subunit alpha isoform 1 (chains A) MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSAD PFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFG MIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGIS LFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLP NLMNLIATIFVFAVVIYFQGFRYELPIRSTKVRGQIGIYPIKLFYTSNIPIILQSALVSN LYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCYYLSPPESFGSVLEDPVH AVVYIVFMLGSCAFFSKTWIEVSGSSPRDIAKQFKDQGMVINGKRETSIYRELKKIIPTA AAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF
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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