Crystal structure of SXN101959, a Clostridium botulinum neurotoxin type D derivative and targeted secretion inhibitor. Determined by X-ray diffraction at 3.1 Å resolution. Released 19 Aug 2015.
Explore 5BQM in 3D Show helices and sheets RCSB PDB PDBe
5BQM contains 80 α-helices and 83 β-strands across 4 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 | 13-14 | 2 | |
| β-strand | 19-23 | 5 | 1 |
| β-strand | 34-40 | 7 | 1 |
| β-strand | 43-45 | 3 | 1 |
| β-strand | 53 | 1 | 2 |
| α-helix | 60-61 | 2 | |
| β-strand | 70 | 1 | 3 |
| β-strand | 72 | 1 | 4 |
| α-helix | 80-97 | 18 | |
| α-helix | 101-112 | 12 | |
| α-helix | 114-116 | 3 | |
| β-strand | 126-128 | 3 | 5 |
| β-strand | 136-141 | 6 | 1 |
| β-strand | 146-152 | 7 | 1 |
| β-strand | 156-159 | 4 | 1 |
| β-strand | 164 | 1 | 4 |
| α-helix | 169-172 | 4 | |
| α-helix | 179-183 | 5 | |
| β-strand | 190-193 | 4 | 1 |
| β-strand | 198-203 | 6 | 6 |
| β-strand | 211 | 1 | 7 |
| β-strand | 215 | 1 | 7 |
| β-strand | 218-220 | 3 | 6 |
| α-helix | 223-238 | 16 | |
| α-helix | 242-244 | 3 | |
| β-strand | 248-249 | 2 | 8 |
| β-strand | 251 | 1 | 9 |
| β-strand | 265-266 | 2 | 8 |
| α-helix | 267-273 | 7 | |
| α-helix | 275-280 | 6 | |
| α-helix | 283-306 | 24 | |
| β-strand | 309-311 | 3 | 5 |
| 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 | 6 |
| β-strand | 394 | 1 | 11 |
| β-strand | 398 | 1 | 11 |
| β-strand | 414 | 1 | 6 |
| β-strand | 422-423 | 2 | 6 |
| α-helix | 424-425 | 2 | |
| β-strand | 430 | 1 | 3 |
| β-strand | 433-437 | 5 | 12 |
| β-strand | 440 | 1 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 511-512 | 2 | 14 |
| β-strand | 513 | 1 | 13 |
| β-strand | 517-520 | 4 | 12 |
| β-strand | 528 | 1 | 9 |
| α-helix | 536-538 | 3 | |
| β-strand | 541-542 | 2 | 15 |
| β-strand | 578-579 | 2 | 1 |
| α-helix | 583-585 | 3 | |
| β-strand | 591 | 1 | 2 |
| α-helix | 592-593 | 2 | |
| α-helix | 595-598 | 4 | |
| β-strand | 599-602 | 4 | 12 |
| α-helix | 608-615 | 8 | |
| α-helix | 617-618 | 2 | |
| β-strand | 625-627 | 3 | 16 |
| α-helix | 630-635 | 6 | |
| β-strand | 639-641 | 3 | 16 |
| α-helix | 645-653 | 9 | |
| α-helix | 660-675 | 16 | |
| β-strand | 679 | 1 | 17 |
| β-strand | 690 | 1 | 17 |
| α-helix | 694-698 | 5 | |
| α-helix | 709-716 | 8 | |
| α-helix | 718-721 | 4 | |
| α-helix | 725-728 | 4 | |
| α-helix | 731-735 | 5 | |
| β-strand | 736-737 | 2 | 15 |
| α-helix | 747-773 | 27 | |
| α-helix | 774-778 | 5 | |
| α-helix | 779-810 | 32 | |
| α-helix | 816-852 | 37 | |
| α-helix | 853-857 | 5 | |
| α-helix | 858-882 | 25 | |
| α-helix | 892-896 | 5 | |
| α-helix | 897-899 | 3 | |
| α-helix | 900-903 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19-23 | 5 | 18 |
| β-strand | 34-40 | 7 | 18 |
| β-strand | 43-45 | 3 | 18 |
| β-strand | 53 | 1 | 19 |
| α-helix | 60-61 | 2 | |
| β-strand | 70-71 | 2 | 20 |
| α-helix | 80-97 | 18 | |
| α-helix | 101-112 | 12 | |
| α-helix | 114-116 | 3 | |
| β-strand | 126-128 | 3 | 21 |
| β-strand | 136-141 | 6 | 18 |
| β-strand | 146-152 | 7 | 18 |
| β-strand | 156-159 | 4 | 18 |
| α-helix | 180-183 | 4 | |
| β-strand | 190-193 | 4 | 18 |
| β-strand | 198-201 | 4 | 22 |
| β-strand | 219 | 1 | 23 |
| β-strand | 220 | 1 | 22 |
| α-helix | 221-222 | 2 | |
| α-helix | 223-239 | 17 | |
| α-helix | 242-244 | 3 | |
| β-strand | 248-249 | 2 | 24 |
| β-strand | 251 | 1 | 25 |
| β-strand | 265-266 | 2 | 24 |
| α-helix | 267-273 | 7 | |
| α-helix | 275-280 | 6 | |
| α-helix | 283-306 | 24 | |
| β-strand | 309-311 | 3 | 21 |
| α-helix | 313-316 | 4 | |
| α-helix | 319-330 | 12 | |
| β-strand | 332-334 | 3 | 26 |
| β-strand | 340-342 | 3 | 26 |
| α-helix | 344-352 | 9 | |
| α-helix | 353-357 | 5 | |
| α-helix | 360-366 | 7 | |
| β-strand | 380-384 | 5 | 22 |
| β-strand | 408 | 1 | 27 |
| β-strand | 410 | 1 | 27 |
| β-strand | 414 | 1 | 23 |
| β-strand | 422-423 | 2 | 22 |
| α-helix | 424-425 | 2 | |
| β-strand | 429-430 | 2 | 20 |
| β-strand | 433-437 | 5 | 28 |
| β-strand | 440-443 | 4 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 510-513 | 4 | 29 |
| β-strand | 517-520 | 4 | 28 |
| α-helix | 525-526 | 2 | |
| β-strand | 528 | 1 | 25 |
| α-helix | 530-532 | 3 | |
| β-strand | 541-542 | 2 | 30 |
| β-strand | 578-579 | 2 | 18 |
| α-helix | 583-585 | 3 | |
| β-strand | 591 | 1 | 19 |
| α-helix | 592-593 | 2 | |
| β-strand | 599-602 | 4 | 28 |
| α-helix | 608-615 | 8 | |
| α-helix | 616-618 | 3 | |
| β-strand | 625-627 | 3 | 31 |
| α-helix | 630-635 | 6 | |
| β-strand | 639-641 | 3 | 31 |
| α-helix | 645-653 | 9 | |
| α-helix | 660-675 | 16 | |
| β-strand | 679-680 | 2 | 32 |
| β-strand | 689-690 | 2 | 32 |
| α-helix | 694-698 | 5 | |
| α-helix | 709-716 | 8 | |
| α-helix | 718-721 | 4 | |
| α-helix | 725-728 | 4 | |
| α-helix | 731-735 | 5 | |
| β-strand | 736-737 | 2 | 30 |
| α-helix | 748-773 | 26 | |
| α-helix | 774-778 | 5 | |
| α-helix | 779-810 | 32 | |
| α-helix | 820-852 | 33 | |
| α-helix | 853-857 | 5 | |
| α-helix | 858-882 | 25 | |
| α-helix | 897-901 | 5 | |
| β-strand | 909-910 | 2 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Botulinum neurotoxin type D | A, C | protein | 453 | Clostridium botulinum | P19321 |
| Somatoliberin,Botulinum neurotoxin type D | B, D | protein | 474 | Homo sapiens, Clostridium botulinum | P01286 (AlphaFold model), P19321 |
>5BQM_1 Botulinum neurotoxin type D (chains A, C) MTWPVKDFNYSDPVNDNDILYLRIPQNKLITTPVKAFMITQNIWVIPERFSSDTNPSLSK PPRPTSKYQSYYDPSYLSTDEQKDTFLKGIIKLFKRINERDIGKKLINYLVVGSPFMGDS STPEDTFDFTRHTTNIAVEKFENGSWKVTNIITPSVLIFGPLPNILDYTASLTLQGQQSN PSFEGFGTLSILKVAPEFLLTFSDVTSNQSSAVLGKSIFCMDPVIALMHELTHSLHQLYG INIPSDKRIRPQVSEGFFSQDGPNVQFEELYTFGGLDVEIIPQIERSQLREKALGHYKDI AKRLNNINKTIPSSWISNIDKYKKIFSEKYNFDKDNTGNFVVNIDKFNSLYSDLTNVMSE VVYSSQYNVKNRTHYFSRHYLPVFANILDDNIYTIRDGFNLTNKGFNIENSGQNIERNPA LQKLSSESVVDLFTKVCVDGIITSKTKSLIEGR
>5BQM_2 Somatoliberin,Botulinum neurotoxin type D (chains B, D) HVDAIFTQSYRKVLAQLSARKLLQDILNRQQGERNQEQGALAGGGGSGGGGSGGGGSALV LQCIKVKNNRLPYVADKDSISQEIFENKIITDETNVQNYSDKFSLDESILDGQVPINPEI VDPLLPNVNMEPLNLPGEEIVFYDDITKYVDYLNSYYYLESQKLSNNVENITLTTSVEEA LGYSNKIYTFLPSLAEKVNKGVQAGLFLNWANEVVEDFTTNIMKKDTLDKISDVSVIIPY IGPALNIGNSALRGNFNQAFATAGVAFLLEGFPEFTIPALGVFTFYSSIQEREKIIKTIE NCLEQRVKRWKDSYQWMVSNWLSRITTQFNHINYQMYDSLSYQADAIKAKIDLEYKKYSG SDKENIKSQVENLKNSLDVKISEAMNNINKFIRECSVTYLFKNMLPKVIDELNKFDLRTK TELINLIDSHNIILVGEVDRLKAKVNESFENTMPFNIFSYTNNSLLKDIINEYF
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
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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