NMR structural studies of a potassium channel / charybdotoxin complex. Determined by solution NMR. Released 10 Jan 2006.
Explore 2A9H in 3D Show helices and sheets RCSB PDB PDBe
2A9H contains 14 α-helices and 2 β-strands across 5 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 | 25-51 | 27 | |
| α-helix | 62-73 | 12 | |
| α-helix | 86-115 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-51 | 27 | |
| β-strand | 55 | 1 | 1 |
| β-strand | 57 | 1 | 1 |
| α-helix | 62-73 | 12 | |
| α-helix | 86-115 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 810-820 | 11 | |
| α-helix | 833-835 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Voltage-gated potassium channel | A, B, C, D | protein | 155 | Streptomyces lividans | P0A334 (AlphaFold model) |
| charybdotoxin | E | protein | 37 | P13487 (AlphaFold model) |
>2A9H_1 Voltage-gated potassium channel (chains A, B, C, D) MSGSHHHHHHSSGIEGRGRLIKHMPPMLSGLLARLVKLLLGRHGSALHWRAAGAATVLLV IVLLAGSYLAVLAERGAPGAALISYPDALWWSVETATTVGYGDLYPVTLWGRCVAVVVMV AGITSYGLVFAAVATWFVGREQERRGHFVRHSEKA
>2A9H_2 charybdotoxin (chains E) QFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS
Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex. Yu, L., Sun, C., Song, D. et al. Biochemistry (2005) 44:15834-15841. DOI 10.1021/bi051656d · PubMed
Other PDB entries of the same protein (UniProt P0A334 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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