Crystal Structure of B. subtilis SecA with bound peptide. Determined by X-ray diffraction at 2.5 Å resolution. Released 24 Nov 2009.
Explore 3JV2 in 3D Show helices and sheets RCSB PDB PDBe
3JV2 contains 80 α-helices and 54 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 | 18-28 | 11 | |
| α-helix | 31-34 | 4 | |
| α-helix | 38-53 | 16 | |
| α-helix | 58-76 | 19 | |
| α-helix | 83-93 | 11 | |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 106-116 | 11 | |
| β-strand | 125-128 | 4 | 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 | |
| β-strand | 203-207 | 5 | 1 |
| α-helix | 209-210 | 2 | |
| α-helix | 211-215 | 5 | |
| α-helix | 219 | 1 | |
| β-strand | 220-228 | 9 | 2 |
| α-helix | 229-230 | 2 | |
| α-helix | 232-243 | 12 | |
| β-strand | 250-253 | 4 | 3 |
| β-strand | 258-261 | 4 | 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 |
| α-helix | 333-340 | 8 | |
| 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 | 5 |
| α-helix | 403-405 | 3 | |
| β-strand | 406-408 | 3 | 6 |
| α-helix | 411-427 | 17 | |
| β-strand | 432-436 | 5 | 5 |
| α-helix | 439-452 | 14 | |
| β-strand | 457-459 | 3 | 5 |
| α-helix | 464-472 | 9 | |
| β-strand | 480-484 | 5 | 5 |
| α-helix | 500-502 | 3 | |
| β-strand | 505-509 | 5 | 5 |
| α-helix | 516-523 | 8 | |
| α-helix | 528-530 | 3 | |
| β-strand | 533-537 | 5 | 5 |
| β-strand | 538-540 | 3 | 6 |
| α-helix | 549-561 | 13 | |
| β-strand | 564 | 1 | 7 |
| β-strand | 567 | 1 | 7 |
| β-strand | 569 | 1 | 6 |
| α-helix | 572-618 | 47 | |
| α-helix | 624-640 | 17 | |
| α-helix | 657-664 | 8 | |
| α-helix | 673-675 | 3 | |
| α-helix | 681-703 | 23 | |
| α-helix | 705-736 | 32 | |
| α-helix | 738-740 | 3 | |
| α-helix | 749-777 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-17 | 3 | |
| α-helix | 18-28 | 11 | |
| α-helix | 30-32 | 3 | |
| α-helix | 38-54 | 17 | |
| α-helix | 58-77 | 20 | |
| α-helix | 83-93 | 11 | |
| β-strand | 97-99 | 3 | 8 |
| α-helix | 106-116 | 11 | |
| β-strand | 125-128 | 4 | 8 |
| α-helix | 131-147 | 17 | |
| β-strand | 152-154 | 3 | 8 |
| α-helix | 161-169 | 9 | |
| β-strand | 172-176 | 5 | 8 |
| α-helix | 177-187 | 11 | |
| α-helix | 193-195 | 3 | |
| β-strand | 203-206 | 4 | 8 |
| α-helix | 209-210 | 2 | |
| α-helix | 211-215 | 5 | |
| α-helix | 219 | 1 | |
| β-strand | 220-228 | 9 | 9 |
| α-helix | 229-230 | 2 | |
| α-helix | 232-243 | 12 | |
| β-strand | 250-253 | 4 | 10 |
| β-strand | 258-261 | 4 | 10 |
| α-helix | 263-273 | 11 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-298 | 15 | |
| β-strand | 302 | 1 | 11 |
| β-strand | 306-308 | 3 | 11 |
| β-strand | 313-315 | 3 | 11 |
| β-strand | 316 | 1 | 12 |
| β-strand | 323 | 1 | 12 |
| α-helix | 333-340 | 8 | |
| α-helix | 343-347 | 5 | |
| β-strand | 349-356 | 8 | 9 |
| α-helix | 357-361 | 5 | |
| β-strand | 366-371 | 6 | 8 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-385 | 8 | |
| β-strand | 389-391 | 3 | 8 |
| α-helix | 392-394 | 3 | |
| β-strand | 401-402 | 2 | 13 |
| α-helix | 403-405 | 3 | |
| β-strand | 406-408 | 3 | 14 |
| α-helix | 411-428 | 18 | |
| β-strand | 432-436 | 5 | 13 |
| α-helix | 439-452 | 14 | |
| β-strand | 457-459 | 3 | 13 |
| α-helix | 464-472 | 9 | |
| β-strand | 480-484 | 5 | 13 |
| α-helix | 499-502 | 4 | |
| β-strand | 505-509 | 5 | 13 |
| α-helix | 516-523 | 8 | |
| α-helix | 528-530 | 3 | |
| β-strand | 533-537 | 5 | 13 |
| β-strand | 538-540 | 3 | 14 |
| α-helix | 544-548 | 5 | |
| α-helix | 552-561 | 10 | |
| β-strand | 564 | 1 | 15 |
| β-strand | 567 | 1 | 15 |
| β-strand | 569 | 1 | 14 |
| α-helix | 572-619 | 48 | |
| α-helix | 624-640 | 17 | |
| α-helix | 657-664 | 8 | |
| α-helix | 681-703 | 23 | |
| α-helix | 705-736 | 32 | |
| α-helix | 738-740 | 3 | |
| α-helix | 749-777 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein translocase subunit SecA | A, B | protein | 783 | Bacillus subtilis | P28366 (AlphaFold model) |
| peptide | C, D | protein | 3 |
>3JV2_1 Protein translocase subunit SecA (chains A, B) GPHMLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGAT TDDLLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLN ALTGKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTN NELGFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQA NAFVRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAH VAMQKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITF QNYFRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKA VAEDVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQK GAVTIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQF YLSMEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLL QYDDVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGL VDLINTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVL RAVDSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMK AEI
>3JV2_2 peptide (chains C, D) XXX
Conformational flexibility and peptide interaction of the translocation ATPase SecA. Zimmer, J., Rapoport, T.A. J Mol Biol (2009) 394:606-612. DOI 10.1016/j.jmb.2009.10.024 · 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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