Active site mutants of B. subtilis SecA. Determined by X-ray diffraction at 3.3 Å resolution. Released 11 Aug 2010.
Explore 3IQY in 3D Show helices and sheets RCSB PDB PDBe
3IQY contains 38 α-helices and 23 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 | 11-28 | 18 | |
| α-helix | 30-34 | 5 | |
| α-helix | 38-53 | 16 | |
| α-helix | 62-76 | 15 | |
| α-helix | 83-94 | 12 | |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 106-117 | 12 | |
| β-strand | 125-128 | 4 | 1 |
| α-helix | 131-147 | 17 | |
| β-strand | 152-154 | 3 | 1 |
| α-helix | 161-167 | 7 | |
| 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 | 231-242 | 12 | |
| α-helix | 263-268 | 6 | |
| α-helix | 285-298 | 14 | |
| β-strand | 306-308 | 3 | 3 |
| β-strand | 313-315 | 3 | 3 |
| β-strand | 316 | 1 | 4 |
| β-strand | 323 | 1 | 4 |
| α-helix | 333-340 | 8 | |
| β-strand | 350-355 | 6 | 2 |
| α-helix | 357-361 | 5 | |
| β-strand | 366-371 | 6 | 1 |
| α-helix | 375-377 | 3 | |
| α-helix | 378-385 | 8 | |
| α-helix | 388 | 1 | |
| β-strand | 389-391 | 3 | 1 |
| β-strand | 401-402 | 2 | 5 |
| α-helix | 403-405 | 3 | |
| β-strand | 406-408 | 3 | 6 |
| α-helix | 411-428 | 18 | |
| β-strand | 432-436 | 5 | 5 |
| α-helix | 439-450 | 12 | |
| β-strand | 457-459 | 3 | 5 |
| α-helix | 464-472 | 9 | |
| β-strand | 480-484 | 5 | 5 |
| α-helix | 492-494 | 3 | |
| β-strand | 505-509 | 5 | 5 |
| α-helix | 516-523 | 8 | |
| β-strand | 533-537 | 5 | 5 |
| β-strand | 538-540 | 3 | 6 |
| α-helix | 544-547 | 4 | |
| α-helix | 552-559 | 8 | |
| β-strand | 569 | 1 | 6 |
| α-helix | 572-618 | 47 | |
| α-helix | 624-642 | 19 | |
| α-helix | 654-664 | 11 | |
| α-helix | 673-676 | 4 | |
| α-helix | 681-702 | 22 | |
| α-helix | 708-737 | 30 | |
| α-helix | 748-777 | 30 | |
| β-strand | 795-797 | 3 | 2 |
| α-helix | 799-801 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein translocase subunit secA | A | protein | 841 | Bacillus subtilis | P28366 (AlphaFold model) |
>3IQY_1 Protein translocase subunit secA (chains A) MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL GFDYLRDNMVLYKEQMVQRPLHFAVIDQVDSILIDEARTPLIISGQAAKSTKLYVQANAF VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV TIATNMAGKGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAEI ENNLEREEVVQGQTTAHQPQEGDDNKKAKKAPVRKVVDIGRNAPCHCGSGKKYKNCCGRT E
ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase. Kim, D.M., Zheng, H., Huang, Y.J. et al. J Am Chem Soc (2013) 135:2999-3010. DOI 10.1021/ja306361q · 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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