1.55 Å crystal structure of wild type diphtheria toxin. Determined by X-ray diffraction at 1.55 Å resolution. Released 16 Nov 2000.
Explore 1F0L in 3D Show helices and sheets RCSB PDB PDBe
1F0L contains 54 α-helices and 66 β-strands across 2 chains. 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 | 2-5 | 4 | |
| β-strand | 6 | 1 | 1 |
| α-helix | 8-10 | 3 | |
| β-strand | 12-15 | 4 | 2 |
| β-strand | 18-23 | 6 | 2 |
| α-helix | 30-33 | 4 | |
| α-helix | 48-50 | 3 | |
| β-strand | 53-56 | 4 | 2 |
| α-helix | 59-63 | 5 | |
| β-strand | 67 | 1 | 3 |
| α-helix | 76 | 1 | |
| β-strand | 77 | 1 | 3 |
| β-strand | 79-84 | 6 | 2 |
| β-strand | 88-93 | 6 | 2 |
| β-strand | 94 | 1 | 1 |
| α-helix | 99-105 | 7 | |
| α-helix | 114-118 | 5 | |
| α-helix | 121-127 | 7 | |
| β-strand | 133-139 | 7 | 2 |
| β-strand | 147-151 | 5 | 2 |
| α-helix | 155-158 | 4 | |
| β-strand | 160-166 | 7 | 2 |
| α-helix | 167-170 | 4 | |
| α-helix | 176-183 | 8 | |
| α-helix | 206-221 | 16 | |
| α-helix | 224-231 | 8 | |
| α-helix | 240-254 | 15 | |
| α-helix | 258-260 | 3 | |
| α-helix | 261-267 | 7 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-288 | 14 | |
| α-helix | 291-294 | 4 | |
| α-helix | 297-304 | 8 | |
| α-helix | 310-314 | 5 | |
| β-strand | 316-317 | 2 | 4 |
| β-strand | 320-321 | 2 | 4 |
| α-helix | 326-347 | 22 | |
| α-helix | 359-375 | 17 | |
| α-helix | 378-380 | 3 | |
| α-helix | 387-388 | 2 | |
| β-strand | 389-391 | 3 | 5 |
| β-strand | 394-398 | 5 | 5 |
| α-helix | 401-404 | 4 | |
| β-strand | 405-407 | 3 | 6 |
| β-strand | 413-422 | 10 | 5 |
| β-strand | 427-429 | 3 | 7 |
| β-strand | 431-435 | 5 | 8 |
| β-strand | 437 | 1 | 5 |
| β-strand | 441-443 | 3 | 5 |
| β-strand | 449-452 | 4 | 5 |
| β-strand | 455-457 | 3 | 5 |
| β-strand | 459-464 | 6 | 8 |
| β-strand | 468-473 | 6 | 8 |
| β-strand | 477-479 | 3 | 7 |
| β-strand | 480 | 1 | 9 |
| β-strand | 483 | 1 | 9 |
| β-strand | 485-493 | 9 | 5 |
| β-strand | 508-518 | 11 | 8 |
| β-strand | 521-530 | 10 | 8 |
| β-strand | 532-534 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| β-strand | 6 | 1 | 10 |
| α-helix | 8-10 | 3 | |
| β-strand | 12-15 | 4 | 2 |
| β-strand | 18-23 | 6 | 2 |
| α-helix | 28-31 | 4 | |
| α-helix | 48-50 | 3 | |
| β-strand | 53-56 | 4 | 2 |
| α-helix | 59-63 | 5 | |
| β-strand | 67 | 1 | 11 |
| α-helix | 76 | 1 | |
| β-strand | 77 | 1 | 11 |
| β-strand | 79-84 | 6 | 2 |
| β-strand | 88-93 | 6 | 2 |
| β-strand | 94 | 1 | 10 |
| α-helix | 99-105 | 7 | |
| α-helix | 114-118 | 5 | |
| α-helix | 121-127 | 7 | |
| β-strand | 133-139 | 7 | 2 |
| β-strand | 147-151 | 5 | 2 |
| α-helix | 155-158 | 4 | |
| β-strand | 160-166 | 7 | 2 |
| α-helix | 168-170 | 3 | |
| α-helix | 176-184 | 9 | |
| α-helix | 206-222 | 17 | |
| α-helix | 224-232 | 9 | |
| α-helix | 240-254 | 15 | |
| α-helix | 258-260 | 3 | |
| α-helix | 261-267 | 7 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-288 | 14 | |
| α-helix | 291-294 | 4 | |
| α-helix | 297-304 | 8 | |
| α-helix | 310-314 | 5 | |
| β-strand | 316-317 | 2 | 12 |
| β-strand | 320-321 | 2 | 12 |
| α-helix | 326-343 | 18 | |
| α-helix | 359-375 | 17 | |
| α-helix | 378-380 | 3 | |
| α-helix | 387-388 | 2 | |
| β-strand | 389-391 | 3 | 13 |
| β-strand | 394-398 | 5 | 13 |
| α-helix | 401-404 | 4 | |
| β-strand | 405-407 | 3 | 14 |
| β-strand | 413-422 | 10 | 13 |
| β-strand | 427-429 | 3 | 15 |
| β-strand | 431-435 | 5 | 16 |
| β-strand | 437 | 1 | 13 |
| β-strand | 441-443 | 3 | 13 |
| β-strand | 449-452 | 4 | 13 |
| β-strand | 455-458 | 4 | 13 |
| β-strand | 459-464 | 6 | 16 |
| β-strand | 468-473 | 6 | 16 |
| β-strand | 477-479 | 3 | 15 |
| β-strand | 480 | 1 | 17 |
| β-strand | 483 | 1 | 17 |
| β-strand | 485-493 | 9 | 13 |
| β-strand | 508-518 | 11 | 16 |
| β-strand | 521-530 | 10 | 16 |
| β-strand | 532-534 | 3 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Diphtheria toxin | A, B | protein | 535 | Corynebacterium diphtheriae | P00588 |
>1F0L_1 DIPHTHERIA TOXIN (chains A, B) GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKY DAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGT EEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYE YMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSE EKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKT TAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNF VESIINLFQVVHNSYNRPAYSPGHKTQPFLHDGYAVSWNTVEDSIIRTGFQGESGHDIKI TAENTPLPIAGVLLPTIPGKLDVNKSKTHISVNGRKIRMRCRAIDGDVTFCRPKSPVYVG NGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNSKLSLFFEIKS
| ID | Name | Formula | Copies |
|---|---|---|---|
| APU | Adenylyl-3'-5'-phospho-uridine-3'-monophosphate | C19 H25 N7 O15 P2 | 2 |
Water and common crystallization additives (CL) are not listed.
Characterization of High-Order Oligomerization and Energetics in Diphtheria Toxin. Steere, B. Thesis (2001). PubMed
Other PDB entries of the same protein (UniProt P00588), best resolution first:
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