Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with an inhibitor (inh2). Determined by X-ray diffraction at 2.17 Å resolution. Released 23 Jun 2009.
Explore 3FII in 3D Show helices and sheets RCSB PDB PDBe
3FII contains 18 α-helices and 26 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 | 3-6 | 4 | |
| α-helix | 13-14 | 2 | |
| β-strand | 19-22 | 4 | 1 |
| α-helix | 23-24 | 2 | |
| α-helix | 28-30 | 3 | |
| β-strand | 34-40 | 7 | 1 |
| β-strand | 43-49 | 7 | 1 |
| α-helix | 56-59 | 4 | |
| β-strand | 63 | 1 | 2 |
| β-strand | 65 | 1 | 2 |
| α-helix | 81-98 | 18 | |
| α-helix | 102-112 | 11 | |
| α-helix | 115-117 | 3 | |
| β-strand | 127 | 1 | 3 |
| β-strand | 136-140 | 5 | 1 |
| β-strand | 146-150 | 5 | 1 |
| β-strand | 153-157 | 5 | 1 |
| β-strand | 166-169 | 4 | 1 |
| β-strand | 172-173 | 2 | 4 |
| β-strand | 179-180 | 2 | 4 |
| α-helix | 182-184 | 3 | |
| β-strand | 191-194 | 4 | 1 |
| β-strand | 199-204 | 6 | 5 |
| β-strand | 216-218 | 3 | 5 |
| α-helix | 221-236 | 16 | |
| β-strand | 247-251 | 5 | 6 |
| β-strand | 259-263 | 5 | 6 |
| α-helix | 264-270 | 7 | |
| α-helix | 272-277 | 6 | |
| α-helix | 280-303 | 24 | |
| β-strand | 306 | 1 | 3 |
| α-helix | 313-323 | 11 | |
| β-strand | 326-328 | 3 | 7 |
| β-strand | 334-336 | 3 | 7 |
| α-helix | 338-348 | 11 | |
| α-helix | 353-360 | 8 | |
| β-strand | 373-376 | 4 | 5 |
| β-strand | 387 | 1 | 8 |
| β-strand | 391 | 1 | 8 |
| α-helix | 395-404 | 10 | |
| β-strand | 405 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-35 | 2 | 1 |
| α-helix | 50-53 | 4 | |
| β-strand | 57 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Botulinum neurotoxin type F | A | protein | 427 | Clostridium botulinum | A7GBG3 (AlphaFold model) |
| fragment of Vesicle-associated membrane protein 2 | B | protein | 33 | P63027 (AlphaFold model) |
>3FII_1 BOTULINUM NEUROTOXIN TYPE F (chains A) MPVVINSFNYNDPVNDDTILYMQIPYEEKSKKYYKAFEIMRNVWIIPERNTIGTDPSDFD PPASLENGSSAYYDPNYLTTDAEKDRYLKTTIKLFKRINSNPAGEVLLQEISYAKPYLGN EHTPINEFHPVTRTTSVNIKSSTNVKSSIILNLLVLGAGPDIFENSSYPVRKLMDSGGVY DPSNDGFGSINIVTFSPEYEYTFNDISGGYNSSTESFIADPAISLAHELIHALHGLYGAR GVTYKETIKVKQAPLMIAEKPIRLEEFLTFGGQDLNIITSAMKEKIYNNLLANYEKIATR LSRVNSAPPEYDINEYKDYFQWKYGLDKNADGSYTVNENKFNEIYKKLYSFTEIDLANKF KVKCRNTYFIKYGFLKVPNLLDDDIYTVSEGFNIGNLAVNNRGQNIKLNPKIIDSIPDKL EHHHHHH
>3FII_2 fragment of Vesicle-associated membrane protein 2 (chains B) TSNRRLQQTQAQVDEVVDIMRVNVDKVLERDCX
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F. Agarwal, R., Schmidt, J.J., Stafford, R.G. et al. Nat Struct Mol Biol (2009) 16:789-794. DOI 10.1038/nsmb.1626 · PubMed
Other PDB entries of the same protein (UniProt A7GBG3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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