Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis. Determined by X-ray diffraction at 3.0 Å resolution. Released 20 Sept 2002.
Explore 1M74 in 3D Show helices and sheets RCSB PDB PDBe
1M74 contains 40 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 | 4-7 | 4 | |
| α-helix | 10-28 | 19 | |
| α-helix | 30-34 | 5 | |
| α-helix | 38-54 | 17 | |
| 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 | 152-155 | 4 | 1 |
| α-helix | 161-169 | 9 | |
| β-strand | 172-176 | 5 | 1 |
| α-helix | 177-186 | 10 | |
| 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 | 221-225 | 5 | 2 |
| α-helix | 232-241 | 10 | |
| β-strand | 250-251 | 2 | 3 |
| β-strand | 258-259 | 2 | 3 |
| α-helix | 263-270 | 8 | |
| α-helix | 279-283 | 5 | |
| α-helix | 284-297 | 14 | |
| β-strand | 306-309 | 4 | 4 |
| β-strand | 312-315 | 4 | 4 |
| β-strand | 316-317 | 2 | 5 |
| β-strand | 322-323 | 2 | 5 |
| α-helix | 330-332 | 3 | |
| α-helix | 333-340 | 8 | |
| α-helix | 343-346 | 4 | |
| β-strand | 350-355 | 6 | 2 |
| α-helix | 357-361 | 5 | |
| β-strand | 366-371 | 6 | 1 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-384 | 7 | |
| 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 | 411-426 | 16 | |
| β-strand | 432-436 | 5 | 6 |
| α-helix | 439-451 | 13 | |
| β-strand | 457-459 | 3 | 6 |
| α-helix | 464-472 | 9 | |
| β-strand | 480-484 | 5 | 6 |
| α-helix | 492-494 | 3 | |
| 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 | 546-548 | 3 | |
| α-helix | 552-560 | 9 | |
| β-strand | 569 | 1 | 7 |
| α-helix | 572-618 | 47 | |
| α-helix | 624-642 | 19 | |
| α-helix | 657-664 | 8 | |
| α-helix | 681-703 | 23 | |
| α-helix | 707-735 | 29 | |
| 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) |
>1M74_1 Preprotein translocase secA (chains A) MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAEI ENNLEREEVVQGQTTAHQPQEG
Water and common crystallization additives (SO4) are not listed.
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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