4I9W: Potassium channel subfamily K member 4
Human two pore domain K+ channel TRAAK (K2P4.1) - Fab complex structure. Determined by X-ray diffraction at 2.75 Å resolution. Released 23 Jan 2013.
- Method
- X-ray diffraction
- Resolution
- 2.75 Å
- Organisms
- Homo sapiens, Mus musculus
- Chains
- 6
- Atoms
- 10,544
- Mol. weight
- 160.47 kDa
- Ligands
- CA
- Released
- 23 Jan 2013
Explore 4I9W in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4I9W contains 51 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, 2 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 | |
| β-strand | 251 | 1 | 1 |
| β-strand | 254 | 1 | 1 |
| α-helix | 257-285 | 29 | |
Chain B: 9 helices, 0 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 | |
| α-helix | 257-283 | 27 | |
Chain D: 8 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 | 144-149 | 6 | 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 | 190-196 | 7 | 6 |
| β-strand | 204-209 | 6 | 6 |
Chain E: 7 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 |
| 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 | 196-202 | 7 | 11 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-213 | 7 | 11 |
Chain F: 9 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 | 121-125 | 5 | |
| 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 |
| β-strand | 204-209 | 6 | 16 |
Chain G: 7 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 |
| 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 | 196-202 | 7 | 21 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-213 | 7 | 21 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Potassium channel subfamily K member 4 | A, B | protein | 309 | Homo sapiens | Q9NYG8 (AlphaFold model) |
| Antibody FAB fragment light chain | D, F | protein | 211 | Mus musculus | |
| Antibody FAB fragment heavy chain | E, G | protein | 217 | Mus musculus | |
Sequence of entity 1 (A, B), FASTA
>4I9W_1 Potassium channel subfamily K member 4 (chains A, B)
MTTAPQEPPARPLQAGSGAGPAPGRAMRSTTLLALLALVLLYLVSGALVFRALEQPHEQQ
AQRELGEVREKFLRAHPCVSDQELGLLIKEVADALGGGADPETQSTSQSSHSAWDLGSAF
FFSGTIITTIGYGNVALRTDAGRLFCIFYALVGIPLFGILLAGVGDRLGSSLRHGIGHIE
AIFLKWHVPPELVRVLSAMLFLLIGCLLFVLTPTFVFCYMEDWSKLEAIYFVIVTLTTVG
FGDYVAGADPRQDSPAYQPLVWFWILLGLAYFASVLTTIGNWLRVVSRRTRAEMGGLTAQ
SNSLEVLFQ
Sequence of entity 2 (D, F), FASTA
>4I9W_2 ANTIBODY FAB FRAGMENT LIGHT CHAIN (chains D, F)
QIVLTQSPAIMSASPGEKVTMTCSASSSVSYMHWYQQKSGTSPKRWIYDTSKLASGVPAR
FSGSGSGTSYSLTISSMEAEDAATYYCQQWSNSPPTFGAGAKLELKRADAAPTVSIFPPS
SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL
TKDEYERHNSYTCEATHKTSTSPIVKSFNRN
Sequence of entity 3 (E, G), FASTA
>4I9W_3 ANTIBODY FAB FRAGMENT HEAVY CHAIN (chains E, G)
EVQLQQSGPELVKPGASMKTSCKVSGYSFTGYIMNWVKQRHGKNLEWIGLINPNTGYTTY
NQKFKGKATLTVDKSSSTAYMELLSLTSEDSAIYYCTRGNYVFDYWGQGTTLTVSSAKTT
PPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTL
SSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 2 |
Water and common crystallization additives (K) are not listed.
Primary citation
Domain-swapped chain connectivity and gated membrane access in a Fab-mediated crystal of the human TRAAK K+ channel. Brohawn, S.G., Campbell, E.B., Mackinnon, R. Proc Natl Acad Sci U S A (2013) 110:2129-2134. DOI 10.1073/pnas.1218950110 · 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
- 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
- 4WFG 3.0 Å, Human TRAAK K+ channel in a Tl+ 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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