Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB). Determined by X-ray diffraction at 2.05 Å resolution. Released 23 Sept 2015.
Explore 4WVG in 3D Show helices and sheets RCSB PDB PDBe
4WVG contains 31 α-helices and 37 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 |
|---|---|---|---|
| β-strand | 13-16 | 4 | 1 |
| α-helix | 23-37 | 15 | |
| β-strand | 41-44 | 4 | 1 |
| α-helix | 49-59 | 11 | |
| β-strand | 65-69 | 5 | 1 |
| α-helix | 70-72 | 3 | |
| α-helix | 73-78 | 6 | |
| β-strand | 82 | 1 | 2 |
| α-helix | 83-85 | 3 | |
| α-helix | 89-92 | 4 | |
| β-strand | 95 | 1 | 3 |
| α-helix | 97-102 | 6 | |
| β-strand | 104-105 | 2 | 4 |
| β-strand | 108-109 | 2 | 4 |
| β-strand | 112-117 | 6 | 1 |
| β-strand | 120-124 | 5 | 5 |
| β-strand | 134 | 1 | 6 |
| α-helix | 135-137 | 3 | |
| α-helix | 138-147 | 10 | |
| β-strand | 151-153 | 3 | 5 |
| α-helix | 160-167 | 8 | |
| β-strand | 173-178 | 6 | 7 |
| β-strand | 181-188 | 8 | 7 |
| α-helix | 192-206 | 15 | |
| α-helix | 216-224 | 9 | |
| β-strand | 228-233 | 6 | 5 |
| α-helix | 235-237 | 3 | |
| α-helix | 238-244 | 7 | |
| β-strand | 248-251 | 4 | 5 |
| α-helix | 252-254 | 3 | |
| β-strand | 255-256 | 2 | 6 |
| β-strand | 259-260 | 2 | 6 |
| α-helix | 261 | 1 | |
| β-strand | 264-265 | 2 | 8 |
| β-strand | 266-272 | 7 | 1 |
| β-strand | 273 | 1 | 2 |
| α-helix | 279-284 | 6 | |
| α-helix | 285-290 | 6 | |
| α-helix | 293-302 | 10 | |
| β-strand | 307-308 | 2 | 1 |
| β-strand | 310 | 1 | 3 |
| α-helix | 311-317 | 7 | |
| α-helix | 321-331 | 11 | |
| β-strand | 334-335 | 2 | 8 |
| α-helix | 336-337 | 2 | |
| α-helix | 342-357 | 16 | |
| α-helix | 363-375 | 13 | |
| β-strand | 378-382 | 5 | 9 |
| β-strand | 397-402 | 6 | 9 |
| α-helix | 403-404 | 2 | |
| β-strand | 415-420 | 6 | 9 |
| β-strand | 424-432 | 9 | 9 |
| β-strand | 437 | 1 | 10 |
| β-strand | 438-441 | 4 | 11 |
| β-strand | 444-447 | 4 | 11 |
| β-strand | 450-452 | 3 | 11 |
| α-helix | 455-457 | 3 | |
| α-helix | 458-462 | 5 | |
| β-strand | 473-474 | 2 | 11 |
| α-helix | 475-477 | 3 | |
| β-strand | 487 | 1 | 10 |
| α-helix | 488-489 | 2 | |
| β-strand | 492-493 | 2 | 12 |
| β-strand | 494-496 | 3 | 9 |
| α-helix | 506-509 | 4 | |
| β-strand | 512-513 | 2 | 12 |
| α-helix | 514-516 | 3 | |
| β-strand | 517-522 | 6 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein,Signal peptidase IB | A | protein | 542 | Escherichia coli K-12, Staphylococcus aureus subsp. aureus str. Newman | P0AEY0 (AlphaFold model) |
>4WVG_1 Maltose-binding periplasmic protein,Signal peptidase IB (chains A) MSYYHHHHHHHMLVIWINGDKGYNGLAQVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG DGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALS LIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENG KYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSN IDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVN KDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGR QTVDEALKDAQTNAGAIVTPYTIKGEAMDPTLKDGERVAVNIVGYKTGGLEKGNVVVFHA NKNDDYVKRVIGVPGDKVEYKNDTLYVNGKKQDEPYLNYNLKHKQGDYITGTFQVKDLPN ANPKSNVIPKGKYLVLGDNREVSKDSRAFGLIDEDQIVGKVSFRFWPFSEFKHNFNPENT KN
Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization. Ting, Y.T., Harris, P.W., Batot, G. et al. IUCrJ (2016) 3:10-19. DOI 10.1107/S2052252515019971 · PubMed
Other PDB entries of the same protein (UniProt P0AEY0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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