Crystal structure of the LHn fragment of botulinum neurotoxin type D, mutant H233Y E230Q. Determined by X-ray diffraction at 2.3 Å resolution. Released 19 Aug 2015.
Explore 5BQN in 3D Show helices and sheets RCSB PDB PDBe
5BQN contains 48 α-helices and 42 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 | 13-14 | 2 | |
| β-strand | 19-23 | 5 | 1 |
| β-strand | 34-40 | 7 | 1 |
| β-strand | 43-46 | 4 | 1 |
| β-strand | 53 | 1 | 2 |
| α-helix | 60-61 | 2 | |
| β-strand | 70 | 1 | 3 |
| α-helix | 80-97 | 18 | |
| α-helix | 101-112 | 12 | |
| α-helix | 114-116 | 3 | |
| β-strand | 126-128 | 3 | 4 |
| β-strand | 136-142 | 7 | 1 |
| β-strand | 145-152 | 8 | 1 |
| β-strand | 156-159 | 4 | 1 |
| α-helix | 170-172 | 3 | |
| α-helix | 176-178 | 3 | |
| α-helix | 179-183 | 5 | |
| β-strand | 190-193 | 4 | 1 |
| β-strand | 198-203 | 6 | 5 |
| β-strand | 211 | 1 | 6 |
| β-strand | 215 | 1 | 6 |
| β-strand | 218-220 | 3 | 5 |
| α-helix | 223-239 | 17 | |
| α-helix | 242-244 | 3 | |
| β-strand | 248-249 | 2 | 7 |
| β-strand | 251 | 1 | 8 |
| β-strand | 254 | 1 | 9 |
| β-strand | 257 | 1 | 9 |
| α-helix | 262-264 | 3 | |
| β-strand | 265-266 | 2 | 7 |
| α-helix | 267-273 | 7 | |
| α-helix | 275-280 | 6 | |
| α-helix | 283-306 | 24 | |
| β-strand | 309-311 | 3 | 4 |
| α-helix | 313-318 | 6 | |
| α-helix | 319-330 | 12 | |
| β-strand | 333-334 | 2 | 10 |
| β-strand | 340-341 | 2 | 10 |
| α-helix | 344-352 | 9 | |
| α-helix | 353-357 | 5 | |
| α-helix | 360-366 | 7 | |
| α-helix | 377-379 | 3 | |
| β-strand | 380-384 | 5 | 5 |
| β-strand | 394 | 1 | 11 |
| β-strand | 398 | 1 | 11 |
| α-helix | 402-404 | 3 | |
| β-strand | 407 | 1 | 12 |
| β-strand | 410 | 1 | 12 |
| β-strand | 414 | 1 | 5 |
| β-strand | 422-423 | 2 | 5 |
| α-helix | 424-425 | 2 | |
| β-strand | 430 | 1 | 3 |
| β-strand | 433-438 | 6 | 13 |
| β-strand | 461-464 | 4 | 13 |
| α-helix | 465-467 | 3 | |
| β-strand | 472 | 1 | 8 |
| α-helix | 474-476 | 3 | |
| α-helix | 480-482 | 3 | |
| β-strand | 485-486 | 2 | 14 |
| β-strand | 522-523 | 2 | 1 |
| α-helix | 524-525 | 2 | |
| α-helix | 527-529 | 3 | |
| β-strand | 535 | 1 | 2 |
| α-helix | 536-537 | 2 | |
| β-strand | 543-547 | 5 | 13 |
| α-helix | 552-558 | 7 | |
| α-helix | 560-562 | 3 | |
| β-strand | 569-571 | 3 | 15 |
| α-helix | 574-579 | 6 | |
| β-strand | 583-585 | 3 | 15 |
| α-helix | 589-596 | 8 | |
| α-helix | 604-619 | 16 | |
| β-strand | 623-624 | 2 | 16 |
| β-strand | 633-634 | 2 | 16 |
| α-helix | 638-642 | 5 | |
| α-helix | 653-660 | 8 | |
| α-helix | 662-665 | 4 | |
| α-helix | 676-679 | 4 | |
| β-strand | 680-681 | 2 | 14 |
| α-helix | 690-692 | 3 | |
| α-helix | 694-717 | 24 | |
| α-helix | 718-722 | 5 | |
| α-helix | 723-754 | 32 | |
| α-helix | 764-772 | 9 | |
| α-helix | 774-795 | 22 | |
| α-helix | 796-801 | 6 | |
| α-helix | 802-826 | 25 | |
| α-helix | 838-842 | 5 | |
| α-helix | 857-859 | 3 | |
| α-helix | 860-870 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Botulinum neurotoxin type D,Botulinum neurotoxin type D | A | protein | 885 | Clostridium botulinum | P19321 |
>5BQN_1 Botulinum neurotoxin type D,Botulinum neurotoxin type D (chains A) MTWPVKDFNYSDPVNDNDILYLRIPQNKLITTPVKAFMITQNIWVIPERFSSDTNPSLSK PPRPTSKYQSYYDPSYLSTDEQKDTFLKGIIKLFKRINERDIGKKLINYLVVGSPFMGDS STPEDTFDFTRHTTNIAVEKFENGSWKVTNIITPSVLIFGPLPNILDYTASLTLQGQQSN PSFEGFGTLSILKVAPEFLLTFSDVTSNQSSAVLGKSIFCMDPVIALMHQLTYSLHQLYG INIPSDKRIRPQVSEGFFSQDGPNVQFEELYTFGGLDVEIIPQIERSQLREKALGHYKDI AKRLNNINKTIPSSWISNIDKYKKIFSEKYNFDKDNTGNFVVNIDKFNSLYSDLTNVMSE VVYSSQYNVKNRTHYFSRHYLPVFANILDDNIYTIRDGFNLTNKGFNIENSGQNIERNPA LQKLSSESVVDLFTKVCVDKSEEKLYDDDDKDRWGSSLQCIKVKNNRLPYVADKDSISQE IFENKIITDETNVQNYSDKFSLDESILDGQVPINPEIVDPLLPNVNMEPLNLPGEEIVFY DDITKYVDYLNSYYYLESQKLSNNVENITLTTSVEEALGYSNKIYTFLPSLAEKVNKGVQ AGLFLNWANEVVEDFTTNIMKKDTLDKISDVSVIIPYIGPALNIGNSALRGNFNQAFATA GVAFLLEGFPEFTIPALGVFTFYSSIQEREKIIKTIENCLEQRVKRWKDSYQWMVSNWLS RITTQFNHINYQMYDSLSYQADAIKAKIDLEYKKYSGSDKENIKSQVENLKNSLDVKISE AMNNINKFIRECSVTYLFKNMLPKVIDELNKFDLRTKTELINLIDSHNIILVGEVDRLKA KVNESFENTMPFNIFSYTNNSLLKDIINEYFNLEAHHHHHHHHHH
Structural analysis of Clostridium botulinum neurotoxin type D as a platform for the development of targeted secretion inhibitors. Masuyer, G., Davies, J.R., Moore, K. et al. Sci Rep (2015) 5:13397-13397. DOI 10.1038/srep13397 · PubMed
Other PDB entries of the same protein (UniProt P19321), best resolution first:
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