Cryo-em of the Sec61-complex bound to the 80s ribosome translating a membrane-inserting substrate. Determined by electron microscopy at 7.8 Å resolution. Released 5 Feb 2014.
Explore 4CG6 in 3D Show helices and sheets RCSB PDB PDBe
4CG6 contains 24 α-helices and 2 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 |
|---|---|---|---|
| α-helix | 28-50 | 23 | |
| α-helix | 64-69 | 6 | |
| α-helix | 82-95 | 14 | |
| α-helix | 114-131 | 18 | |
| α-helix | 149-170 | 22 | |
| α-helix | 180-196 | 17 | |
| α-helix | 201 | 1 | |
| α-helix | 204 | 1 | |
| α-helix | 215-221 | 7 | |
| α-helix | 242-257 | 16 | |
| β-strand | 263 | 1 | 1 |
| β-strand | 281 | 1 | 1 |
| α-helix | 288-311 | 24 | |
| α-helix | 317-322 | 6 | |
| α-helix | 338 | 1 | |
| α-helix | 341-345 | 5 | |
| α-helix | 350-352 | 3 | |
| α-helix | 361-379 | 19 | |
| α-helix | 387-396 | 10 | |
| α-helix | 416-439 | 24 | |
| α-helix | 447-462 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-24 | 17 | |
| α-helix | 31-58 | 28 | |
| α-helix | 59-61 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 70-85 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-16 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein transport protein SEC61 subunit alpha isoform 1 | A | protein | 476 | CANIS LUPUS FAMILIARIS | P38377 (AlphaFold model) |
| Protein transport protein SEC61 subunit gamma | B | protein | 68 | CANIS LUPUS FAMILIARIS | P60058 (AlphaFold model) |
| Protein transport protein SEC61 subunit beta | C | protein | 96 | CANIS LUPUS FAMILIARIS | P60467 (AlphaFold model) |
| Peptide | D | protein | 17 | CANIS LUPUS FAMILIARIS |
>4CG6_1 PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT ALPHA ISOFORM 1 (chains A) MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSAD PFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFG MIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGIS LFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLP NLMNLIATIFVFAVVIYFQGFRVDLPIKSARYRGQYNTYPIKLFYTSNIPIILQSALVSN LYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCHYLSPPESFGSVLEDPVH AVVYIVFMLGSCAFFSKTWIEVSGSSAKDVAKQLKEQQMVMRGHRETSMVHELNRYIPTA AAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF
>4CG6_2 PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT GAMMA (chains B) MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIP INNIIVGG
>4CG6_3 PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT BETA (chains C) MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYT EDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS
>4CG6_4 PEPTIDE (chains D) VFIVSVGSFISVLFIVI
Structures of the Sec61 Complex Engaged in Nascent Peptide Translocation or Membrane Insertion. Gogala, M., Becker, T., Beatrix, B. et al. Nature (2014) 506:107. DOI 10.1038/NATURE12950 · PubMed
Other PDB entries of the same protein (UniProt P38377 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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