Structure of the SecA-SecY complex with the substrate HmBRI-7TM. Determined by electron microscopy at 3.97 Å resolution. Released 26 Feb 2025.
Explore 8YAS in 3D Show helices and sheets RCSB PDB PDBe
8YAS contains 61 α-helices and 31 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 | 15-32 | 18 | |
| α-helix | 43-54 | 12 | |
| α-helix | 62-76 | 15 | |
| α-helix | 83-93 | 11 | |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 100-101 | 2 | |
| α-helix | 106-117 | 12 | |
| β-strand | 124-128 | 5 | 1 |
| α-helix | 131-148 | 18 | |
| β-strand | 152-154 | 3 | 1 |
| α-helix | 161-168 | 8 | |
| β-strand | 172-176 | 5 | 1 |
| α-helix | 177-187 | 11 | |
| α-helix | 193-195 | 3 | |
| β-strand | 203-207 | 5 | 1 |
| α-helix | 209 | 1 | |
| α-helix | 210-215 | 6 | |
| α-helix | 216-218 | 3 | |
| β-strand | 220-226 | 7 | 2 |
| α-helix | 232-241 | 10 | |
| α-helix | 245-249 | 5 | |
| β-strand | 250-253 | 4 | 3 |
| β-strand | 258-261 | 4 | 3 |
| α-helix | 263-272 | 10 | |
| α-helix | 284-294 | 11 | |
| α-helix | 295-299 | 5 | |
| α-helix | 302-305 | 4 | |
| β-strand | 306-309 | 4 | 4 |
| β-strand | 312-316 | 5 | 4 |
| α-helix | 317 | 1 | |
| β-strand | 323-324 | 2 | 4 |
| α-helix | 333-341 | 9 | |
| β-strand | 349-356 | 8 | 2 |
| α-helix | 357-361 | 5 | |
| β-strand | 367-371 | 5 | 1 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-383 | 6 | |
| β-strand | 389-391 | 3 | 1 |
| β-strand | 400-402 | 3 | 5 |
| α-helix | 403-405 | 3 | |
| β-strand | 406-408 | 3 | 6 |
| α-helix | 411-426 | 16 | |
| β-strand | 432-435 | 4 | 5 |
| α-helix | 439-450 | 12 | |
| β-strand | 456-459 | 4 | 5 |
| α-helix | 464-466 | 3 | |
| α-helix | 467-473 | 7 | |
| β-strand | 480-483 | 4 | 5 |
| α-helix | 493-495 | 3 | |
| α-helix | 499-501 | 3 | |
| β-strand | 506-509 | 4 | 5 |
| α-helix | 516-527 | 12 | |
| β-strand | 533-537 | 5 | 5 |
| β-strand | 538-540 | 3 | 6 |
| α-helix | 544-549 | 6 | |
| α-helix | 554-556 | 3 | |
| α-helix | 573-618 | 46 | |
| α-helix | 624-641 | 18 | |
| α-helix | 654-664 | 11 | |
| α-helix | 673-675 | 3 | |
| α-helix | 681-703 | 23 | |
| α-helix | 706-741 | 36 | |
| α-helix | 742-744 | 3 | |
| α-helix | 748-776 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| β-strand | 19 | 1 | 9 |
| α-helix | 23-58 | 36 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-8 | 6 | |
| α-helix | 12-32 | 21 | |
| β-strand | 35 | 1 | 7 |
| α-helix | 36 | 1 | |
| α-helix | 41-46 | 6 | |
| β-strand | 57-60 | 4 | 8 |
| β-strand | 63-66 | 4 | 8 |
| β-strand | 68 | 1 | 7 |
| α-helix | 75-88 | 14 | |
| α-helix | 93-101 | 9 | |
| α-helix | 105-136 | 32 | |
| α-helix | 146-172 | 27 | |
| α-helix | 178-201 | 24 | |
| α-helix | 213-235 | 23 | |
| β-strand | 238-242 | 5 | 9 |
| β-strand | 244-245 | 2 | 10 |
| β-strand | 261-265 | 5 | 9 |
| α-helix | 272-289 | 18 | |
| α-helix | 295-303 | 9 | |
| α-helix | 309-330 | 22 | |
| α-helix | 333-343 | 11 | |
| β-strand | 345-346 | 2 | 10 |
| α-helix | 354-387 | 34 | |
| α-helix | 400-420 | 21 | |
| α-helix | 421-423 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein translocase subunit SecA | A | protein | 778 | Bacillus subtilis subsp. subtilis str. 168 | P28366 (AlphaFold model) |
| Protein translocase subunit SecY | Y | protein | 430 | Geobacillus thermodenitrificans NG80-2 | A4IJK8 (AlphaFold model) |
| Protein translocase subunit SecE | E | protein | 70 | Geobacillus thermodenitrificans NG80-2 | A4IJH4 (AlphaFold model) |
>8YAS_1 Protein translocase subunit SecA (chains A) MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKA
>8YAS_2 Protein translocase subunit SecY (chains Y) MFRTISNFMRVSDIRNKIIFTLLMLIVFRIGTFIPVPSVNTDVLKLQDQLNAFGVLNIFC GGALQNFSIFAMGVMPYITASIIVQLLQMDVVPKFAEWSKQGEMGRRKLAQFTRYFTIVL GFIQALGMSYGFNNLAGGMLIQNPGIGTYLLIAVVLTAGTAFLMWLGEQITAKGVGNGIS IIIFAGIVSGIPTILNQIYAQTFENVGEDLTLNIVRLLLVALAVVAVIVGVIYIQQAFRK IPIQYAKRLEGRNPVGGHSTHLPLKVNPAGVIPVIFAVSFLIAPPTIASFFGTNDVTLWI RRTFDYTHPVGMTIYVVLIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGIRPGKNTQEYV TRILYRLTLVGSLFLAFIAVLPVFFVNFANLPPSAQIGGTSLLIVVGVALETMKQLESQL VKRHYRGFIK
>8YAS_3 Protein translocase subunit SecE (chains E) MQRVTNFFKEVVRELKKVSWPNRKELVNYTAVVLATVAFFTVFFAVIDLGISQLIRLVFE GGHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| BEF | Beryllium trifluoride ion | Be F3 | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
SecY translocon chaperones protein folding during membrane protein insertion. Ou, X., Ma, C., Sun, D. et al. Cell (2025) 188:1912-1924.e13. DOI 10.1016/j.cell.2025.01.037 · PubMed
Other PDB entries of the same protein (UniProt P28366 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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