Structural Classification of Proteins
Protein: Bungarotoxin from Many-banded krait (Bungarus multicinctus), Alpha-bungarotoxin
[TaxId: 8616]
Lineage:
Root:
scop
Class:
Small proteins
[56992]
Usually dominated by metal ligand, heme, and/or disulfide bridges
Fold:
Snake toxin-like
[57301]
disulfide-rich fold: nearly all-beta
Superfamily:
Snake toxin-like
[57302]
uperfamily
Family:
Snake venom toxins
[57303]
Protein: Bungarotoxin [57324]
Species:
Many-banded krait (Bungarus multicinctus), Alpha-bungarotoxin
[TaxId: 8616]
[57325]
PDB Entry Domains:
1hc9
complexed with high affinity peptide
complexed with ido
chain a
[65786]
chain b
[65787]
2qc1
automatically matched to d1hc9a_
complexed with man, nag; mutant
region a:1-74
[150650]
2abx
chain a
[44424]
chain b
[44425]
1kfh
chain a
[72412]
1ikc
complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
chain a
[62526]
1abt
chain a
[44426]
1jbd
complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
chain a
[62844]
1haj
complexed with a high affinity 13-mer peptide
chain a
[60878]
1ljz
complexed with an ACHR peptide, chain B
chain a
[73947]
1haa
complexed with a high affinity 13-mer peptide
chain a
[60877]
1idi
chain a
[62298]
1bxp
chain a
[44428]
1hoy
complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
chain a
[44429]
1kc4
complex with the principal binding sequence on the alpha7 subunit of a neuronal nicotinic acetylcholine receptor, chain B
chain a
[72293]
2btx
chain a
[44430]
1idh
complexed to an 18mer cognate peptide
chain a
[62297]
1idl
chain a
[62299]
1rgj
complexed with a mimotope of the nicotinic acetylcholine receptor, chain B
chain a
[97439]
1l4w
complexed with an ACHR peptide, chain B
chain a
[73570]
1idg
complexed to an 18mer cognate peptide
chain a
[62296]
1kl8
complex with the principal binding sequence on the alpha7 subunit of a neuronal nicotinic acetylcholine receptor, chain B
chain a
[72680]
1ik8
chain a
[62525]
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Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright
© 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk