Crystal structure of SecA in an open conformation from Bacillus Subtilis. Determined by X-ray diffraction at 2.18 Å resolution. Released 3 Aug 2004.
Explore 1TF5 in 3D Show helices and sheets RCSB PDB PDBe
1TF5 contains 43 α-helices and 25 β-strands across 1 chain. 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 | 1-6 | 6 | |
| α-helix | 18-28 | 11 | |
| α-helix | 31-34 | 4 | |
| α-helix | 38-53 | 16 | |
| α-helix | 58-77 | 20 | |
| α-helix | 83-93 | 11 | |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 106-118 | 13 | |
| β-strand | 124-128 | 5 | 1 |
| α-helix | 131-147 | 17 | |
| β-strand | 152-154 | 3 | 1 |
| α-helix | 161-169 | 9 | |
| β-strand | 172-176 | 5 | 1 |
| α-helix | 177-187 | 11 | |
| α-helix | 193-195 | 3 | |
| α-helix | 198-200 | 3 | |
| β-strand | 203-207 | 5 | 1 |
| α-helix | 209-210 | 2 | |
| α-helix | 211-215 | 5 | |
| β-strand | 220-228 | 9 | 2 |
| α-helix | 232-241 | 10 | |
| β-strand | 250 | 1 | 3 |
| β-strand | 261 | 1 | 3 |
| α-helix | 263-272 | 10 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-298 | 15 | |
| β-strand | 302 | 1 | 4 |
| β-strand | 306-309 | 4 | 4 |
| β-strand | 312-315 | 4 | 4 |
| β-strand | 316 | 1 | 5 |
| β-strand | 323 | 1 | 5 |
| α-helix | 333-340 | 8 | |
| α-helix | 347-348 | 2 | |
| β-strand | 349-356 | 8 | 2 |
| α-helix | 357-361 | 5 | |
| β-strand | 366-371 | 6 | 1 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-385 | 8 | |
| β-strand | 389-391 | 3 | 1 |
| α-helix | 392-394 | 3 | |
| β-strand | 401-402 | 2 | 6 |
| α-helix | 403-405 | 3 | |
| β-strand | 406-408 | 3 | 7 |
| α-helix | 411-428 | 18 | |
| β-strand | 432-436 | 5 | 6 |
| α-helix | 439-450 | 12 | |
| β-strand | 457-459 | 3 | 6 |
| α-helix | 464-471 | 8 | |
| β-strand | 480-484 | 5 | 6 |
| α-helix | 494-496 | 3 | |
| α-helix | 500-502 | 3 | |
| β-strand | 505-509 | 5 | 6 |
| α-helix | 516-523 | 8 | |
| α-helix | 528-530 | 3 | |
| β-strand | 533-537 | 5 | 6 |
| β-strand | 538-540 | 3 | 7 |
| α-helix | 545-547 | 3 | |
| α-helix | 550-561 | 12 | |
| β-strand | 569 | 1 | 7 |
| α-helix | 572-618 | 47 | |
| α-helix | 624-641 | 18 | |
| α-helix | 657-662 | 6 | |
| α-helix | 667 | 1 | |
| α-helix | 681-697 | 17 | |
| α-helix | 698-702 | 5 | |
| α-helix | 707-736 | 30 | |
| α-helix | 738-740 | 3 | |
| α-helix | 748-776 | 29 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Preprotein translocase secA subunit | A | protein | 844 | Bacillus subtilis | P28366 (AlphaFold model) |
>1TF5_1 Preprotein translocase secA subunit (chains A) GPHMLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGAT TDDLLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLN ALTGKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTN NELGFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQA NAFVRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAH VAMQKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITF QNYFRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKA VAEDVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQK GAVTIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQF YLSMEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLL QYDDVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGL VDLINTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVL RAVDSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMK AEIENNLEREEVVQGQTTAHQPQEGDDNKKAKKAPVRKVVDIGRNAPCHCGSGKKYKNCC GRTE
A large conformational change of the translocation ATPase SecA. Osborne, A.R., Clemons Jr., W.M., Rapoport, T.A. Proc Natl Acad Sci U S A (2004) 101:10937-10942. DOI 10.1073/pnas.0401742101 · 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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