Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.45-A resolution. Determined by X-ray diffraction at 1.45 Å resolution. Released 26 Oct 2011.
Explore 3TEW in 3D Show helices and sheets RCSB PDB PDBe
3TEW contains 29 α-helices and 58 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 | 19-24 | 6 | 1 |
| β-strand | 32-38 | 7 | 1 |
| β-strand | 42 | 1 | 2 |
| β-strand | 45 | 1 | 3 |
| α-helix | 47-49 | 3 | |
| α-helix | 55-57 | 3 | |
| β-strand | 59 | 1 | 4 |
| β-strand | 62-70 | 9 | 1 |
| β-strand | 75-77 | 3 | 5 |
| β-strand | 78-81 | 4 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 87-91 | 5 | 1 |
| β-strand | 94-98 | 5 | 1 |
| β-strand | 106-108 | 3 | 5 |
| β-strand | 113-121 | 9 | 1 |
| β-strand | 129 | 1 | 4 |
| β-strand | 130 | 1 | 3 |
| β-strand | 133 | 1 | 2 |
| β-strand | 134-137 | 4 | 6 |
| β-strand | 143-145 | 3 | 6 |
| α-helix | 146-147 | 2 | |
| α-helix | 148-150 | 3 | |
| β-strand | 151-152 | 2 | 1 |
| α-helix | 185-190 | 6 | |
| β-strand | 192-196 | 5 | 1 |
| β-strand | 201-205 | 5 | 1 |
| α-helix | 208-211 | 4 | |
| β-strand | 219 | 1 | 1 |
| α-helix | 235-240 | 6 | |
| α-helix | 249-252 | 4 | |
| β-strand | 256 | 1 | 7 |
| β-strand | 262-273 | 12 | 8 |
| α-helix | 274-275 | 2 | |
| α-helix | 284-286 | 3 | |
| β-strand | 289-292 | 4 | 8 |
| β-strand | 293-297 | 5 | 9 |
| β-strand | 328-334 | 7 | 9 |
| α-helix | 346-350 | 5 | |
| β-strand | 357-368 | 12 | 8 |
| β-strand | 374 | 1 | 10 |
| α-helix | 378-380 | 3 | |
| β-strand | 381-385 | 5 | 9 |
| β-strand | 389-394 | 6 | 9 |
| β-strand | 405 | 1 | 10 |
| β-strand | 409-411 | 3 | 8 |
| β-strand | 419-420 | 2 | 8 |
| α-helix | 429-431 | 3 | |
| β-strand | 432-435 | 4 | 8 |
| α-helix | 436-445 | 10 | |
| β-strand | 447-452 | 6 | 9 |
| β-strand | 458-463 | 6 | 11 |
| β-strand | 468-476 | 9 | 11 |
| α-helix | 477-479 | 3 | |
| α-helix | 481-487 | 7 | |
| β-strand | 488-493 | 6 | 7 |
| β-strand | 501-506 | 6 | 7 |
| β-strand | 508 | 1 | 12 |
| α-helix | 513-517 | 5 | |
| α-helix | 519-520 | 2 | |
| β-strand | 522 | 1 | 13 |
| α-helix | 523-531 | 9 | |
| β-strand | 534 | 1 | 14 |
| β-strand | 541-542 | 2 | 14 |
| β-strand | 545-546 | 2 | 14 |
| α-helix | 547-549 | 3 | |
| β-strand | 550-554 | 5 | 7 |
| α-helix | 556-568 | 13 | |
| α-helix | 574-576 | 3 | |
| α-helix | 581 | 1 | |
| β-strand | 582 | 1 | 13 |
| α-helix | 583 | 1 | |
| β-strand | 584 | 1 | 12 |
| β-strand | 588-593 | 6 | 7 |
| β-strand | 596-598 | 3 | 15 |
| β-strand | 604-607 | 4 | 15 |
| α-helix | 609-615 | 7 | |
| β-strand | 619-623 | 5 | 16 |
| β-strand | 626-629 | 4 | 16 |
| α-helix | 633-637 | 5 | |
| β-strand | 639-647 | 9 | 17 |
| β-strand | 653-655 | 3 | 17 |
| β-strand | 666-668 | 3 | 16 |
| β-strand | 674-677 | 4 | 16 |
| β-strand | 695-702 | 8 | 17 |
| α-helix | 703-705 | 3 | |
| β-strand | 724-730 | 7 | 17 |
| α-helix | 731-734 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protective antigen | A | protein | 715 | Bacillus anthracis | P13423 (AlphaFold model) |
>3TEW_1 Protective antigen (chains A) EVKQENRLLNESESSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYF QSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINKASNSNKIRLEKGRLYQIKIQY QRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSNSRKKRSTSAGPTVPDRDN DGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVT GRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHT SEPGSNSNSSTVAIDHSLSLAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPT TSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPIALNAQDDFSSTPITMNYNQFL ELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNWSEVLPQIQETTARIIFNGKDLNL VERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTSQ NIKNQLAELNATNIYTVLDKIKLNAKMNILIRDKRFHYDRNNIAVGADESVVKEAHREVI NSSTEGLLLNIDKDIRKILSGYIVEIEDTEGLKEVINDRYDMLNISSLRQDGKTFIDFKK YNDKLPLYISNPNYKVNVYAVTKENTIINPSENGDTSTNGIKKILIFSKKGYEIG
Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen. Feld, G.K., Kintzer, A.F., Tang, I.I. et al. J Mol Biol (2012) 415:159-174. DOI 10.1016/j.jmb.2011.10.035 · PubMed
Other PDB entries of the same protein (UniProt P13423 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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