Structure of the SecA/SecYE/proOmpA(4Y)-sfGFP complex with ADP.BeF3-. Determined by electron microscopy at 3.35 Å resolution. Released 11 Jan 2023.
Explore 7XHA in 3D Show helices and sheets RCSB PDB PDBe
7XHA contains 59 α-helices and 30 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 | 16-28 | 13 | |
| α-helix | 29-32 | 4 | |
| α-helix | 38-52 | 15 | |
| α-helix | 59-61 | 3 | |
| α-helix | 62-77 | 16 | |
| α-helix | 83-93 | 11 | |
| β-strand | 98-99 | 2 | 1 |
| α-helix | 108-117 | 10 | |
| β-strand | 124-128 | 5 | 2 |
| α-helix | 131-148 | 18 | |
| β-strand | 152-154 | 3 | 2 |
| α-helix | 161-168 | 8 | |
| β-strand | 172-176 | 5 | 2 |
| α-helix | 177-187 | 11 | |
| α-helix | 198-201 | 4 | |
| β-strand | 203-207 | 5 | 2 |
| α-helix | 209 | 1 | |
| α-helix | 210-215 | 6 | |
| α-helix | 220 | 1 | |
| β-strand | 221-225 | 5 | 3 |
| α-helix | 232-241 | 10 | |
| β-strand | 250-252 | 3 | 4 |
| β-strand | 259-261 | 3 | 4 |
| 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 | 5 |
| β-strand | 312-315 | 4 | 5 |
| β-strand | 316 | 1 | 6 |
| α-helix | 317 | 1 | |
| β-strand | 323 | 1 | 6 |
| β-strand | 327-329 | 3 | 3 |
| α-helix | 334-340 | 7 | |
| α-helix | 346-348 | 3 | |
| β-strand | 350-355 | 6 | 3 |
| α-helix | 357-361 | 5 | |
| β-strand | 366-370 | 5 | 2 |
| α-helix | 378-384 | 7 | |
| α-helix | 388-389 | 2 | |
| β-strand | 390-391 | 2 | 1 |
| β-strand | 401-402 | 2 | 7 |
| α-helix | 403-405 | 3 | |
| α-helix | 411-426 | 16 | |
| β-strand | 432-435 | 4 | 7 |
| α-helix | 440-450 | 11 | |
| β-strand | 457-459 | 3 | 7 |
| α-helix | 465-472 | 8 | |
| β-strand | 480-483 | 4 | 7 |
| β-strand | 506-509 | 4 | 7 |
| α-helix | 516-526 | 11 | |
| β-strand | 534-537 | 4 | 7 |
| α-helix | 544-549 | 6 | |
| α-helix | 552-557 | 6 | |
| α-helix | 558-561 | 4 | |
| α-helix | 574-618 | 45 | |
| α-helix | 624-642 | 19 | |
| α-helix | 654-664 | 11 | |
| α-helix | 681-703 | 23 | |
| α-helix | 707-736 | 30 | |
| α-helix | 739-744 | 6 | |
| α-helix | 748-777 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-19 | 17 | |
| β-strand | 50-53 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-14 | 12 | |
| β-strand | 19 | 1 | 8 |
| α-helix | 23-57 | 35 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-8 | 5 | |
| α-helix | 12-32 | 21 | |
| α-helix | 43-46 | 4 | |
| α-helix | 75-87 | 13 | |
| α-helix | 93-100 | 8 | |
| α-helix | 106-135 | 30 | |
| α-helix | 147-173 | 27 | |
| α-helix | 178-187 | 10 | |
| α-helix | 191-201 | 11 | |
| α-helix | 217-235 | 19 | |
| β-strand | 238-241 | 4 | 8 |
| β-strand | 244 | 1 | 9 |
| β-strand | 262-265 | 4 | 8 |
| α-helix | 272-290 | 19 | |
| α-helix | 295-303 | 9 | |
| α-helix | 309-330 | 22 | |
| α-helix | 333-343 | 11 | |
| β-strand | 346 | 1 | 9 |
| β-strand | 347 | 1 | 10 |
| β-strand | 350 | 1 | 10 |
| α-helix | 355-389 | 35 | |
| α-helix | 400-421 | 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 | 60 | Geobacillus thermodenitrificans NG80-2 | A4IJH4 (AlphaFold model) |
| Translocating polypeptide | B | protein | 303 | Escherichia coli |
>7XHA_1 Protein translocase subunit SecA (chains A) MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKA
>7XHA_2 Protein translocase subunit SecY (chains Y) MFRTISNFMRVSDIRNKIIFTLLMLIVFRIGTFIPVPSVNTDVLKLQDQLNAFGVLNIFC GGALQNFSIFAMGVMPYITASIIVQLLQMDVVPKFAEWSKQGEMGRRKLAQFTRYFTIVL GFIQALGMSYGFNNLAGGMLIQNPGIGTYLLIAVVLTAGTAFLMWLGEQITAKGVGNGIS IIIFAGIVSGIPTILNQIYAQQFENVGEDLFLRIVRLLLVALAVVAVIVGVIYIQQAFRK IPIQYAKRLEGRNPVGGHSTHLPLKVNPAGVIPVIFAVSFLIAPPTIASFFGTNDVTLWI RRTFDYTHPVGMTIYVVLIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGIRPGKNTQEYV TRILYRLTLVGSLFLAFIAVLPVFFVNFANLPPSAQIGGTSLLIVVGVALETMKQLESQL VKRHYRGFIK
>7XHA_3 Protein translocase subunit SecE (chains E) MQRVTNFFKEVVRELKKVSWPNRKELVNYTAVVLATVAFFTVFFAVIDLGISQLIRLVFE
>7XHA_4 Translocating polypeptide (chains B) MAKKTAIAIAVALAGFATVASYAQYEDGCSGELERQHTFAGGARSIASGYYYYSGDKLPE GVLQSGGSGSKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGK LPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEV KFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVE DGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHG SAG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| BEF | Beryllium trifluoride ion | Be F3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Structural basis of SecA-mediated protein translocation. Dong, L., Yang, S., Chen, J. et al. Proc Natl Acad Sci U S A (2023) 120:e2208070120-e2208070120. DOI 10.1073/pnas.2208070120 · 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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