6B8L: Apo/CaM:Kv7.4 (KCNQ4) AB Domain Complex
Crystal Structure of the Apo/CaM:Kv7.4 (KCNQ4) AB Domain Complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 14 Mar 2018.
- Method
- X-ray diffraction
- Resolution
- 2.3 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 7,260
- Mol. weight
- 107.55 kDa
- Released
- 14 Mar 2018
Explore 6B8L in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6B8L contains 55 α-helices and 17 β-strands across 8 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: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 339-354 | 16 | |
| α-helix | 359-361 | 3 | |
| α-helix | 364-526 | 9 | |
| α-helix | 528-550 | 23 | |
Chain B: 9 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-19 | 14 | |
| β-strand | 26-27 | 2 | 1 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-53 | 9 | |
| β-strand | 63-64 | 2 | 1 |
| α-helix | 65-74 | 10 | |
| α-helix | 79-91 | 13 | |
| β-strand | 99-101 | 3 | 2 |
| α-helix | 102-111 | 10 | |
| α-helix | 115-117 | 3 | |
| α-helix | 118-127 | 10 | |
| β-strand | 135-137 | 3 | 2 |
| α-helix | 138-145 | 8 | |
Chain C: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 331-334 | 4 | |
| α-helix | 339-354 | 16 | |
| α-helix | 359-361 | 3 | |
| α-helix | 364-526 | 9 | |
| α-helix | 528-551 | 24 | |
Chain D: 9 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-19 | 12 | |
| β-strand | 26-27 | 2 | 3 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-55 | 11 | |
| β-strand | 63-64 | 2 | 3 |
| α-helix | 65-74 | 10 | |
| α-helix | 79-90 | 12 | |
| β-strand | 99-101 | 3 | 4 |
| α-helix | 102-111 | 10 | |
| α-helix | 115-117 | 3 | |
| α-helix | 118-128 | 11 | |
| β-strand | 135-137 | 3 | 4 |
| α-helix | 138-145 | 8 | |
Chain E: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 335-353 | 19 | |
| α-helix | 359-361 | 3 | |
| α-helix | 364-526 | 9 | |
| α-helix | 528-550 | 23 | |
Chain F: 9 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-19 | 14 | |
| β-strand | 27 | 1 | 5 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-53 | 9 | |
| β-strand | 63 | 1 | 5 |
| α-helix | 65-74 | 10 | |
| α-helix | 79-91 | 13 | |
| β-strand | 99-101 | 3 | 6 |
| α-helix | 102-111 | 10 | |
| α-helix | 115-117 | 3 | |
| α-helix | 118-127 | 10 | |
| β-strand | 130 | 1 | 6 |
| β-strand | 135-137 | 3 | 6 |
| α-helix | 138-145 | 8 | |
Chain G: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 335-354 | 20 | |
| α-helix | 359-361 | 3 | |
| α-helix | 364-526 | 9 | |
| α-helix | 528-550 | 23 | |
| α-helix | 551-553 | 3 | |
Chain H: 10 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-5 | 3 | |
| α-helix | 6-19 | 14 | |
| β-strand | 26-27 | 2 | 7 |
| α-helix | 29-38 | 10 | |
| α-helix | 45-53 | 9 | |
| β-strand | 63-64 | 2 | 7 |
| α-helix | 65-74 | 10 | |
| α-helix | 79-91 | 13 | |
| β-strand | 99-101 | 3 | 8 |
| α-helix | 102-111 | 10 | |
| α-helix | 115-117 | 3 | |
| α-helix | 118-127 | 10 | |
| β-strand | 135-137 | 3 | 8 |
| α-helix | 138-145 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Potassium voltage-gated channel subfamily KQT member 4 | A, C, E, G | protein | 82 | Homo sapiens | P56696 (AlphaFold model) |
| Calmodulin-1 | B, D, F, H | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>6B8L_1 Potassium voltage-gated channel subfamily KQT member 4 (chains A, C, E, G)
GHMKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDMSRAYLTATWYKLDDIMPAVKTVIR
SIRILKFLVAKRKFKETLRPYD
Sequence of entity 2 (B, D, F, H), FASTA
>6B8L_2 Calmodulin-1 (chains B, D, F, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK
Primary citation
A Calmodulin C-Lobe Ca2+-Dependent Switch Governs Kv7 Channel Function. Chang, A., Abderemane-Ali, F., Hura, G.L. et al. Neuron (2018) 97:836-852.e6. DOI 10.1016/j.neuron.2018.01.035 · PubMed
Other PDB entries of the same protein (UniProt P56696 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2OVC 2.07 Å, Crystal structure of a coiled-coil tetramerization domain from Kv7.4 channels
- 6N5W 2.15 Å, Crystal structure of the Ca2+/CaM complex with independent peptides of Kv7.4 (KCNQ4) A &…
- 6B8P 2.2 Å, Crystal Structure of the Mg2+/CaM:Kv7.4 (KCNQ4) AB domain complex
- 6B8N 2.2 Å, Crystal Structure of the Ca2+/CaM:Kv7.4 (KCNQ4) AB Domain Complex, 10 uM CaCl2 soak
- 6B8M 2.3 Å, Crystal Structure of the Ca2+/CaM:Kv7.4 (KCNQ4) AB Domain Complex, 1 mM CaCl2 soak
- 7BYL 2.5 Å, Cryo-EM structure of human KCNQ4
- 4GOW 2.6 Å, Crystal Structure of Ca2+/CaM:Kv7.4 (KCNQ4) B helix complex
- 7VNP 2.79 Å, Structure of human KCNQ4-ML213 complex with PIP2
- 7VNR 2.8 Å, Structure of human KCNQ4-ML213 complex in digitonin
- 7VNQ 2.96 Å, Structure of human KCNQ4-ML213 complex in nanodisc
- 7BYM 3.1 Å, Cryo-EM structure of human KCNQ4 with retigabine
- 7BYN 3.3 Å, Cryo-EM structure of human KCNQ4 with linopirdine
Browse structure collections
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