4WFG: Potassium channel subfamily K member 4
Human TRAAK K+ channel in a Tl+ bound conductive conformation. Determined by X-ray diffraction at 3.0 Å resolution. Released 3 Dec 2014.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organisms
- Homo sapiens, Mus musculus
- Chains
- 6
- Atoms
- 10,599
- Mol. weight
- 159.92 kDa
- Ligands
- CA, TL
- Released
- 3 Dec 2014
Explore 4WFG in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4WFG contains 55 α-helices and 87 β-strands across 6 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: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-54 | 26 | |
| α-helix | 55-57 | 3 | |
| α-helix | 60-75 | 16 | |
| α-helix | 81-96 | 16 | |
| α-helix | 116-127 | 12 | |
| α-helix | 140-185 | 46 | |
| α-helix | 190-205 | 16 | |
| α-helix | 206-211 | 6 | |
| α-helix | 212-221 | 10 | |
| α-helix | 225-236 | 12 | |
| α-helix | 257-285 | 29 | |
Chain B: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-75 | 47 | |
| α-helix | 81-96 | 16 | |
| α-helix | 116-127 | 12 | |
| α-helix | 140-185 | 46 | |
| α-helix | 190-205 | 16 | |
| α-helix | 206-211 | 6 | |
| α-helix | 212-221 | 10 | |
| α-helix | 225-236 | 12 | |
| β-strand | 251 | 1 | 1 |
| β-strand | 254 | 1 | 1 |
| α-helix | 257-285 | 29 | |
Chain D: 9 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-5 | 2 | 2 |
| β-strand | 10-13 | 4 | 3 |
| β-strand | 19-25 | 7 | 2 |
| β-strand | 33-37 | 5 | 3 |
| β-strand | 44-48 | 5 | 3 |
| β-strand | 52-53 | 2 | 3 |
| α-helix | 54 | 1 | |
| β-strand | 61-66 | 6 | 2 |
| β-strand | 69-74 | 6 | 2 |
| α-helix | 79-81 | 3 | |
| β-strand | 83-89 | 7 | 3 |
| α-helix | 95 | 1 | |
| β-strand | 96-97 | 2 | 3 |
| β-strand | 101-105 | 5 | 3 |
| β-strand | 110 | 1 | 4 |
| α-helix | 111-112 | 2 | |
| β-strand | 113-117 | 5 | 5 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-125 | 5 | |
| β-strand | 128-138 | 11 | 5 |
| β-strand | 139 | 1 | 4 |
| β-strand | 143-149 | 7 | 6 |
| β-strand | 152-154 | 3 | 6 |
| β-strand | 158-162 | 5 | 5 |
| α-helix | 163-166 | 4 | |
| β-strand | 172-181 | 10 | 5 |
| α-helix | 182-187 | 6 | |
| β-strand | 190-197 | 8 | 6 |
| α-helix | 203 | 1 | |
| β-strand | 204-209 | 6 | 6 |
Chain E: 8 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 7 |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 45-51 | 7 | 8 |
| β-strand | 58-60 | 3 | 8 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 7 |
| β-strand | 78-83 | 6 | 7 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 8 |
| β-strand | 105-106 | 2 | 8 |
| β-strand | 110-114 | 5 | 8 |
| α-helix | 117-119 | 3 | |
| β-strand | 120 | 1 | 9 |
| α-helix | 121-122 | 2 | |
| β-strand | 123-127 | 5 | 10 |
| β-strand | 138-148 | 11 | 10 |
| β-strand | 149 | 1 | 9 |
| β-strand | 154-157 | 4 | 11 |
| α-helix | 158-160 | 3 | |
| β-strand | 166-168 | 3 | 10 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 10 |
| β-strand | 177-187 | 11 | 10 |
| β-strand | 197-202 | 6 | 11 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-212 | 6 | 11 |
Chain F: 10 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-5 | 2 | 12 |
| β-strand | 10-13 | 4 | 13 |
| β-strand | 19-25 | 7 | 12 |
| β-strand | 33-37 | 5 | 13 |
| β-strand | 44-48 | 5 | 13 |
| β-strand | 52-53 | 2 | 13 |
| α-helix | 54 | 1 | |
| β-strand | 61-66 | 6 | 12 |
| β-strand | 69-74 | 6 | 12 |
| α-helix | 79-81 | 3 | |
| β-strand | 83-89 | 7 | 13 |
| α-helix | 95 | 1 | |
| β-strand | 96-97 | 2 | 13 |
| β-strand | 101-105 | 5 | 13 |
| α-helix | 106 | 1 | |
| β-strand | 110 | 1 | 14 |
| α-helix | 111-112 | 2 | |
| β-strand | 113-117 | 5 | 15 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-126 | 6 | |
| β-strand | 128-138 | 11 | 15 |
| β-strand | 139 | 1 | 14 |
| β-strand | 144-149 | 6 | 16 |
| β-strand | 152-154 | 3 | 16 |
| β-strand | 158-162 | 5 | 15 |
| α-helix | 163-166 | 4 | |
| β-strand | 172-181 | 10 | 15 |
| α-helix | 182-187 | 6 | |
| β-strand | 190-196 | 7 | 16 |
| α-helix | 203 | 1 | |
| β-strand | 204-209 | 6 | 16 |
Chain G: 8 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 17 |
| β-strand | 10-12 | 3 | 18 |
| β-strand | 18-25 | 8 | 17 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 18 |
| β-strand | 45-51 | 7 | 18 |
| β-strand | 58-60 | 3 | 18 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 17 |
| β-strand | 78-83 | 6 | 17 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 18 |
| β-strand | 105-106 | 2 | 18 |
| β-strand | 110-114 | 5 | 18 |
| α-helix | 117-119 | 3 | |
| β-strand | 120 | 1 | 19 |
| α-helix | 121-122 | 2 | |
| β-strand | 123-127 | 5 | 20 |
| β-strand | 138-148 | 11 | 20 |
| β-strand | 149 | 1 | 19 |
| β-strand | 154-157 | 4 | 21 |
| α-helix | 158-160 | 3 | |
| β-strand | 162 | 1 | 21 |
| β-strand | 166-168 | 3 | 20 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 20 |
| β-strand | 177-187 | 11 | 20 |
| β-strand | 197-202 | 6 | 21 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-212 | 6 | 21 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Potassium channel subfamily K member 4 | A, B | protein | 299 | Homo sapiens | Q9NYG8 (AlphaFold model) |
| Anti-traak antibody 13E9 FAB fragment light chain | D, F | protein | 211 | Mus musculus | |
| Anti-traak antibody 13E9 FAB fragment heavy chain | E, G | protein | 217 | Mus musculus | |
Sequence of entity 1 (A, B), FASTA
>4WFG_1 Potassium channel subfamily K member 4 (chains A, B)
MTTAPQEPPARPLQAGSGAGPAPGRAMRSTTLLALLALVLLYLVSGALVFRALEQPHEQQ
AQRELGEVREKFLRAHPCVSDQELGLLIKEVADALGGGADPETQSTSQSSHSAWDLGSAF
FFSGTIITTIGYGNVALRTDAGRLFCIFYALVGIPLFGILLAGVGDRLGSSLRHGIGHIE
AIFLKWHVPPELVRVLSAMLFLLIGCLLFVLTPTFVFCYMEDWSKLEAIYFVIVTLTTVG
FGDYVAGADPRQDSPAYQPLVWFWILLGLAYFASVLTTIGNWLRVVSRRTSNSLEVLFQ
Sequence of entity 2 (D, F), FASTA
>4WFG_2 ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT LIGHT CHAIN (chains D, F)
QIVLTQSPAIMSASPGEKVTMTCSASSSVSYMHWYQQKSGTSPKRWIYDTSKLASGVPAR
FSGSGSGTSYSLTISSMEAEDAATYYCQQWSNSPPTFGAGAKLELKRADAAPTVSIFPPS
SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL
TKDEYERHNSYTCEATHKTSTSPIVKSFNRN
Sequence of entity 3 (E, G), FASTA
>4WFG_3 ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT HEAVY CHAIN (chains E, G)
EVQLQQSGPELVKPGASMKTSCKVSGYSFTGYIMNWVKQRHGKNLEWIGLINPNTGYTTY
NQKFKGKATLTVDKSSSTAYMELLSLTSEDSAIYYCTRGNYVFDYWGQGTTLTVSSAKTT
PPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTL
SSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 3 |
| TL | Thallium (I) ion | Tl | 8 |
Primary citation
Physical mechanism for gating and mechanosensitivity of the human TRAAK K+ channel. Brohawn, S.G., Campbell, E.B., MacKinnon, R. Nature (2014) 516:126-130. DOI 10.1038/nature14013 · PubMed
Other PDB entries of the same protein (UniProt Q9NYG8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7LJ5 2.26 Å, Human TRAAK K+ channel FHIEG mutant A198E in a K+ bound conductive conformation
- 4WFE 2.5 Å, Human TRAAK K+ channel in a K+ bound conductive conformation
- 4WFF 2.5 Å, Human TRAAK K+ channel in a K+ bound nonconductive conformation
- 4I9W 2.75 Å, Human two pore domain K+ channel TRAAK (K2P4.1) - Fab complex structure
- 7LJA 2.77 Å, Human TRAAK K+ channel FHEIG mutant A198E in a Tl+ bound conductive conformation
- 7LJ4 2.78 Å, Human TRAAK K+ channel FHEIG mutant A270P in a K+ bound conductive conformation
- 7LJB 2.97 Å, Human TRAAK K+ channel mutant G158D in a K+ bound conductive conformation
- 4WFH 3.01 Å, Human TRAAK K+ channel in a Tl+ bound nonconductive conformation
- 4RUE 3.3 Å, Human K2P4.1 (TRAAK) potassium channel, G124I mutant
- 3UM7 3.31 Å, Crystal structure of the human two pore domain K+ ion channel TRAAK (K2P4.1)
- 4RUF 3.4 Å, Human K2P4.1 (TRAAAK) potassium channel, W262S mutant
Browse structure collections
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