Crystal structure of the SecA translocation ATPase from Bacillus subtilis. Determined by X-ray diffraction at 2.7 Å resolution. Released 20 Sept 2002.
Explore 1M6N in 3D Show helices and sheets RCSB PDB PDBe
1M6N contains 41 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 | 4-9 | 6 | |
| α-helix | 10-28 | 19 | |
| α-helix | 31-34 | 4 | |
| α-helix | 38-53 | 16 | |
| α-helix | 58-77 | 20 | |
| α-helix | 83-94 | 12 | |
| 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 | |
| β-strand | 203-207 | 5 | 1 |
| α-helix | 209 | 1 | |
| α-helix | 210-214 | 5 | |
| α-helix | 215-217 | 3 | |
| β-strand | 221-226 | 6 | 2 |
| α-helix | 231-241 | 11 | |
| β-strand | 250 | 1 | 3 |
| β-strand | 259 | 1 | 3 |
| α-helix | 264-267 | 4 | |
| α-helix | 270-272 | 3 | |
| α-helix | 279-283 | 5 | |
| α-helix | 284-298 | 15 | |
| α-helix | 302-305 | 4 | |
| β-strand | 306-307 | 2 | 4 |
| β-strand | 314-315 | 2 | 4 |
| β-strand | 316 | 1 | 5 |
| β-strand | 323 | 1 | 5 |
| α-helix | 330-332 | 3 | |
| α-helix | 333-340 | 8 | |
| β-strand | 349-355 | 7 | 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 | 403-404 | 2 | |
| β-strand | 406-408 | 3 | 7 |
| α-helix | 411-426 | 16 | |
| β-strand | 432-436 | 5 | 6 |
| α-helix | 439-451 | 13 | |
| β-strand | 457-459 | 3 | 6 |
| α-helix | 464-472 | 9 | |
| α-helix | 473-475 | 3 | |
| β-strand | 480-484 | 5 | 6 |
| α-helix | 499-502 | 4 | |
| β-strand | 507-509 | 3 | 6 |
| α-helix | 516-524 | 9 | |
| β-strand | 534-537 | 4 | 6 |
| β-strand | 538-540 | 3 | 7 |
| α-helix | 552-560 | 9 | |
| β-strand | 569 | 1 | 7 |
| α-helix | 572-618 | 47 | |
| α-helix | 624-641 | 18 | |
| α-helix | 649-651 | 3 | |
| α-helix | 656-664 | 9 | |
| α-helix | 681-702 | 22 | |
| α-helix | 707-734 | 28 | |
| α-helix | 748-777 | 30 | |
| β-strand | 794-797 | 4 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Preprotein translocase secA | A | protein | 802 | Bacillus subtilis | P28366 (AlphaFold model) |
>1M6N_1 Preprotein translocase secA (chains A) MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAEI ENNLEREEVVQGQTTAHQPQEG
Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA. Hunt, J.F., Weinkauf, S., Henry, L. et al. Science (2002) 297:2018-2026. DOI 10.1126/science.1074424 · 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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