2ISH: Neurotoxin BoNT/A

Botulinum Neurotoxin A Light Chain WT Crystal Form C. Determined by X-ray diffraction at 2.0 Å resolution. Released 7 Nov 2006.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Clostridium botulinum
Chains
2
Atoms
7,027
Mol. weight
96.46 kDa
Ligands
ZN
Released
7 Nov 2006

Explore 2ISH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ISH contains 41 α-helices and 50 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.

Chain A: 21 helices, 25 β-strands

ElementResiduesLengthSheet
α-helix13-142
β-strand19-2351
α-helix30-323
β-strand33-3971
β-strand42-4871
α-helix54-563
α-helix60-634
α-helix64-663
β-strand7312
α-helix81-9919
α-helix102-11312
α-helix115-1173
β-strand11913
β-strand126-12724
β-strand12813
α-helix131-1333
β-strand134-13851
β-strand144-14851
β-strand151-15551
β-strand15912
β-strand164-16631
β-strand184-18741
β-strand192-19875
β-strand211-21445
α-helix217-23216
α-helix236-2383
β-strand242-24326
β-strand258-25926
α-helix260-2667
α-helix268-2714
α-helix276-29924
β-strand302-30324
α-helix310-32112
β-strand324-32527
β-strand331-33227
α-helix335-3439
α-helix344-3485
α-helix351-3588
β-strand372-37545
β-strand38518
β-strand38918
α-helix396-3983
α-helix402-4043
β-strand40515
α-helix410-4123
β-strand414-41525
Chain B: 20 helices, 25 β-strands
ElementResiduesLengthSheet
β-strand19-2359
β-strand33-3979
β-strand42-4879
α-helix54-563
α-helix60-634
α-helix64-663
β-strand73110
α-helix81-9919
α-helix102-11312
α-helix115-1173
β-strand119111
β-strand126-127212
β-strand128111
α-helix131-1333
β-strand134-13859
α-helix1391
β-strand144-14859
β-strand151-15559
β-strand159110
β-strand164-16639
β-strand184-18749
β-strand192-198713
β-strand211-214413
α-helix217-23216
α-helix236-2383
β-strand242-244314
β-strand257-259314
α-helix260-2667
α-helix268-2725
α-helix276-29924
β-strand302-303212
α-helix310-32112
β-strand324-325215
β-strand331-332215
α-helix335-3439
α-helix344-3485
α-helix351-3588
β-strand372-375413
β-strand385116
β-strand389116
α-helix396-3983
α-helix402-4043
β-strand405113
α-helix410-4123
β-strand414-415213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Neurotoxin BoNT/AA, Bprotein421Clostridium botulinumP0DPI0 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2ISH_1 Neurotoxin BoNT/A (chains A, B)
PFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNP
PPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGS
TIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYG
STQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNR
VFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAK
SIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVL
NRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTP
G

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

Inhibition of metalloprotease botulinum serotype A from a pseudo-peptide binding mode to a small molecule that is active in primary neurons. Burnett, J.C., Ruthel, G., Stegmann, C.M. et al. J Biol Chem (2007) 282:5004-5014. DOI 10.1074/jbc.M608166200 · PubMed

Other PDB entries of the same protein (UniProt P0DPI0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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