Cs+ complex of a K channel with an amide to ester substitution in the selectivity filter. Determined by X-ray diffraction at 2.75 Å resolution. Released 12 Sept 2006.
Explore 2HG5 in 3D Show helices and sheets RCSB PDB PDBe
2HG5 contains 18 α-helices and 44 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 4-5 | 2 | 1 |
| β-strand | 9-12 | 4 | 2 |
| β-strand | 18-24 | 7 | 1 |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-52 | 8 | 2 |
| β-strand | 57-60 | 4 | 2 |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 2 |
| β-strand | 107-108 | 2 | 2 |
| β-strand | 112-116 | 5 | 2 |
| β-strand | 122 | 1 | 3 |
| α-helix | 123-124 | 2 | |
| β-strand | 125-128 | 4 | 4 |
| α-helix | 130-132 | 3 | |
| β-strand | 140-150 | 11 | 4 |
| β-strand | 151 | 1 | 3 |
| β-strand | 156-159 | 4 | 5 |
| β-strand | 168-170 | 3 | 4 |
| α-helix | 171-173 | 3 | |
| β-strand | 174 | 1 | 4 |
| β-strand | 180-189 | 10 | 4 |
| α-helix | 190-192 | 3 | |
| β-strand | 199 | 1 | 6 |
| β-strand | 200-204 | 5 | 5 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-211 | 3 | 5 |
| β-strand | 214 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-6 | 3 | 7 |
| β-strand | 10-13 | 4 | 8 |
| β-strand | 18-25 | 8 | 7 |
| β-strand | 33-38 | 6 | 8 |
| β-strand | 45-49 | 5 | 8 |
| α-helix | 50-52 | 3 | |
| β-strand | 53-54 | 2 | 8 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 7 |
| β-strand | 70-76 | 7 | 7 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 8 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 8 |
| β-strand | 102-106 | 5 | 8 |
| β-strand | 111 | 1 | 9 |
| β-strand | 114-118 | 5 | 10 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 130-139 | 10 | 10 |
| β-strand | 140 | 1 | 9 |
| β-strand | 144-150 | 7 | 11 |
| β-strand | 153-155 | 3 | 11 |
| β-strand | 159-163 | 5 | 10 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-181 | 9 | 10 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 11 |
| β-strand | 201-210 | 10 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-51 | 28 | |
| α-helix | 62-73 | 12 | |
| α-helix | 86-118 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FAB heavy chain | A | protein | 219 | Mus musculus | Q569B4 (AlphaFold model) |
| FAB light chain | B | protein | 212 | Mus musculus | P01837 (AlphaFold model) |
| Kcsa channel | C | protein | 101 | synthetic construct | P0A334 (AlphaFold model) |
>2HG5_1 FAB HEAVY CHAIN (chains A) QVQLQQPGAELVKPGASVKLSCKASGYTFTSDWIHWVKQRPGHGLEWIGEIIPSYGRANY NEKIQKKATLTADKSSSTAFMQLSSLTSEDSAVYYCARERGDGYFAVWGAGTTVTVSSAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD
>2HG5_2 FAB LIGHT CHAIN (chains B) DILLTQSPAILSVSPGERVSFSCRASQSIGTDIHWYQQRTNGSPRLLIKYASESISGIPS RFSGSGSGTDFTLSINSVESEDIANYYCQQSNRWPFTFGSGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRN
>2HG5_3 KCSA CHANNEL (chains C) SALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWACETATTVGYXDL YPVTLWGRLVAVVVMVAGITSFGLVTAALATWFVGREQERR
Structural and Functional Consequences of an Amide-to-Ester Substitution in the Selectivity Filter of a Potassium Channel. Valiyaveetil, F.I., Sekedat, M., Mackinnon, R. et al. J Am Chem Soc (2006) 128:11591-11599. DOI 10.1021/ja0631955 · PubMed
Other PDB entries of the same protein (UniProt Q569B4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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