Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+1C). Determined by electron microscopy at 3.29 Å resolution. Released 26 Feb 2025.
Explore 8Y9Y in 3D Show helices and sheets RCSB PDB PDBe
8Y9Y contains 62 α-helices and 33 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 | 16-33 | 18 | |
| α-helix | 36-37 | 2 | |
| α-helix | 42-54 | 13 | |
| α-helix | 60-77 | 18 | |
| α-helix | 83-93 | 11 | |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 112-116 | 5 | |
| β-strand | 124-128 | 5 | 2 |
| α-helix | 131-147 | 17 | |
| β-strand | 152-154 | 3 | 2 |
| α-helix | 161-167 | 7 | |
| β-strand | 172-176 | 5 | 2 |
| α-helix | 177-187 | 11 | |
| α-helix | 193-195 | 3 | |
| α-helix | 198-201 | 4 | |
| β-strand | 203-206 | 4 | 2 |
| β-strand | 207 | 1 | 1 |
| α-helix | 209 | 1 | |
| α-helix | 210-215 | 6 | |
| α-helix | 216-218 | 3 | |
| β-strand | 220-226 | 7 | 3 |
| α-helix | 232-241 | 10 | |
| β-strand | 250-253 | 4 | 4 |
| β-strand | 258-261 | 4 | 4 |
| α-helix | 263-272 | 10 | |
| α-helix | 284-298 | 15 | |
| α-helix | 302-305 | 4 | |
| β-strand | 307-308 | 2 | 5 |
| β-strand | 313-314 | 2 | 5 |
| β-strand | 315-316 | 2 | 6 |
| α-helix | 317 | 1 | |
| β-strand | 323-324 | 2 | 6 |
| β-strand | 327-329 | 3 | 3 |
| α-helix | 334-340 | 7 | |
| α-helix | 343-345 | 3 | |
| β-strand | 349-356 | 8 | 3 |
| α-helix | 357-361 | 5 | |
| β-strand | 367 | 1 | 2 |
| β-strand | 369-371 | 3 | 1 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-383 | 6 | |
| β-strand | 389-391 | 3 | 1 |
| β-strand | 400-402 | 3 | 7 |
| β-strand | 406-408 | 3 | 8 |
| α-helix | 411-426 | 16 | |
| β-strand | 432-435 | 4 | 7 |
| α-helix | 439-450 | 12 | |
| β-strand | 456-459 | 4 | 7 |
| α-helix | 467-471 | 5 | |
| β-strand | 480-483 | 4 | 7 |
| α-helix | 485-488 | 4 | |
| α-helix | 500-502 | 3 | |
| β-strand | 506-509 | 4 | 7 |
| α-helix | 516-527 | 12 | |
| β-strand | 533-537 | 5 | 7 |
| β-strand | 538-540 | 3 | 8 |
| α-helix | 544-549 | 6 | |
| α-helix | 555-561 | 7 | |
| β-strand | 569 | 1 | 8 |
| α-helix | 572-618 | 47 | |
| α-helix | 624-641 | 18 | |
| α-helix | 654-664 | 11 | |
| α-helix | 673-675 | 3 | |
| α-helix | 681-703 | 23 | |
| α-helix | 705-737 | 33 | |
| α-helix | 740-742 | 3 | |
| α-helix | 748-776 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-19 | 16 | |
| α-helix | 37-42 | 6 | |
| α-helix | 46-50 | 5 | |
| β-strand | 64-66 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-17 | 14 | |
| β-strand | 19 | 1 | 9 |
| α-helix | 23-58 | 36 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-10 | 7 | |
| α-helix | 12-30 | 19 | |
| α-helix | 35-36 | 2 | |
| α-helix | 43-45 | 3 | |
| α-helix | 75-88 | 14 | |
| α-helix | 93-101 | 9 | |
| α-helix | 103-136 | 34 | |
| α-helix | 146-173 | 28 | |
| α-helix | 178-201 | 24 | |
| α-helix | 215-235 | 21 | |
| β-strand | 238-242 | 5 | 9 |
| β-strand | 244 | 1 | 10 |
| β-strand | 261-265 | 5 | 9 |
| α-helix | 272-291 | 20 | |
| α-helix | 296-303 | 8 | |
| α-helix | 309-330 | 22 | |
| α-helix | 333-342 | 10 | |
| β-strand | 346 | 1 | 10 |
| α-helix | 354-379 | 26 | |
| α-helix | 381-389 | 9 | |
| α-helix | 401-422 | 22 |
| 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) |
| Substrate FtsQ-LacY(+1C) | B | protein | 73 | Escherichia coli K-12 | P02920 (AlphaFold model), P06136 |
>8Y9Y_1 Protein translocase subunit SecA (chains A) MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKA
>8Y9Y_2 Protein translocase subunit SecY (chains Y) MFRTISNFMRVSDIRNKIIFTLLMLIVFRIGTFIPVPSVNTDVLKLQDQLNAFGVLNIFC GGALQNFSIFAMGVMPYITASIIVQLLQMDVVPKFAEWSKQGEMGRRKLAQFTRYFTIVL GFIQALGMSYGFNNLAGGMLIQNPGIGTYLLIAVVLTAGTAFLMWLGEQITAKGVGNGIS IIIFAGIVSGIPTILNQIYAQTFENVGEDLTLNIVRLLLVALAVVAVIVGVIYIQQAFRK IPIQYAKRLEGRNPVGGHSTHLPLKVNPAGVIPVIFAVSFLIAPPTIASFFGTNDVTLWI RRTFDYTHPVGMTIYVVLIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGIRPGKNTQEYV TRILYRLTLVGSLFLAFIAVLPVFFVNFANLPPSAQIGGTSLLIVVGVALETMKQLESQL VKRHYRGFIK
>8Y9Y_3 Protein translocase subunit SecE (chains E) MQRVTNFFKEVVRELKKVSWPNRKELVNYTAVVLATVAFFTVFFAVIDLGISQLIRLVFE GGHHHHHHHH
>8Y9Y_4 Substrate FtsQ-LacY(+1C) (chains B) MAKKTILFLLTVLTTVLVSGWVVLGCQYEDGSSGVVILKTLHMFEVPFLLVGAFSISGDG DSPHSYHSGDGDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| BEF | Beryllium trifluoride ion | Be F3 | 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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