Crystal structure of the catalytic domain of botulinum neurotoxin BoNT/A C134 mutant with MTSEA modified Cys-165 causing stretch disorder. Determined by X-ray diffraction at 1.7 Å resolution. Released 9 Jul 2014.
Explore 4KUF in 3D Show helices and sheets RCSB PDB PDBe
4KUF contains 19 α-helices and 23 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 |
| α-helix | 30-32 | 3 | |
| β-strand | 33-39 | 7 | 1 |
| β-strand | 42-48 | 7 | 1 |
| β-strand | 73 | 1 | 2 |
| α-helix | 81-99 | 19 | |
| α-helix | 102-113 | 12 | |
| α-helix | 115-117 | 3 | |
| β-strand | 119 | 1 | 3 |
| β-strand | 126-128 | 3 | 3 |
| α-helix | 131-133 | 3 | |
| β-strand | 134-138 | 5 | 1 |
| β-strand | 144-148 | 5 | 1 |
| β-strand | 151-155 | 5 | 1 |
| β-strand | 159 | 1 | 2 |
| β-strand | 184-187 | 4 | 1 |
| β-strand | 192-196 | 5 | 4 |
| α-helix | 200-203 | 4 | |
| β-strand | 213-214 | 2 | 4 |
| α-helix | 215-216 | 2 | |
| α-helix | 217-232 | 16 | |
| β-strand | 242-244 | 3 | 5 |
| α-helix | 249-253 | 5 | |
| β-strand | 257-259 | 3 | 5 |
| α-helix | 260-266 | 7 | |
| α-helix | 270-273 | 4 | |
| α-helix | 276-299 | 24 | |
| β-strand | 302-304 | 3 | 3 |
| α-helix | 310-320 | 11 | |
| β-strand | 324-325 | 2 | 6 |
| β-strand | 331-332 | 2 | 6 |
| α-helix | 335-343 | 9 | |
| α-helix | 344-348 | 5 | |
| α-helix | 351-358 | 8 | |
| β-strand | 372-375 | 4 | 4 |
| β-strand | 385 | 1 | 7 |
| β-strand | 389 | 1 | 7 |
| α-helix | 402-404 | 3 | |
| β-strand | 405 | 1 | 4 |
| α-helix | 410-412 | 3 | |
| β-strand | 414-418 | 5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Botulinum neurotoxin A light chain | A | protein | 445 | Clostridium botulinum A | P0DPI1 (AlphaFold model) |
>4KUF_1 Botulinum neurotoxin A light chain (chains A) MGSSHHHHHHSSGLVPRGSHMPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHN KIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYS TDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNSINVIQPDGSYRSEELNLVIIGPSADI IQFEXKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVT LAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQEN EFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDK LYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAAN FNGQNTEINNMNFTKLKNFTGLFEF
Water and common crystallization additives (NA, EDO, GOL, DMS) are not listed.
Covalent modification of the active site cysteine stresses Clostridium botulinum neurotoxin A. Guitot, K., Vera, L., Le Roux, L. et al. To be published.
Other PDB entries of the same protein (UniProt P0DPI1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4KUF directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.