8J01: Human KCNQ2-CaM
Human KCNQ2-CaM in complex with CBD and PIP2. Determined by electron microscopy at 3.1 Å resolution. Released 13 Dec 2023.
- Method
- Electron microscopy
- Resolution
- 3.1 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 16,232
- Mol. weight
- 378.47 kDa
- Ligands
- P0T, PIO
- Released
- 13 Dec 2023
Explore 8J01 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8J01 contains 95 α-helices and 8 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: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 71-85 | 15 | |
| α-helix | 91-114 | 24 | |
| α-helix | 119-147 | 29 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 196-210 | 15 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-253 | 25 | |
| α-helix | 259-261 | 3 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-347 | 60 | |
| α-helix | 357-366 | 10 | |
| α-helix | 536-558 | 23 | |
| α-helix | 564-599 | 36 | |
Chain B: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 71-85 | 15 | |
| α-helix | 91-114 | 24 | |
| α-helix | 119-147 | 29 | |
| α-helix | 156-163 | 8 | |
| α-helix | 167-183 | 17 | |
| α-helix | 196-210 | 15 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-253 | 25 | |
| α-helix | 259-261 | 3 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-347 | 60 | |
| α-helix | 357-366 | 10 | |
| α-helix | 536-558 | 23 | |
| α-helix | 564-599 | 36 | |
Chain C: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| α-helix | 66-74 | 9 | |
| α-helix | 77-80 | 4 | |
| α-helix | 83-93 | 11 | |
| β-strand | 101 | 1 | 1 |
| α-helix | 103-110 | 8 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137 | 1 | 1 |
| α-helix | 139-147 | 9 | |
Chain D: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 71-85 | 15 | |
| α-helix | 91-114 | 24 | |
| α-helix | 119-147 | 29 | |
| α-helix | 156-163 | 8 | |
| α-helix | 167-183 | 17 | |
| α-helix | 196-210 | 15 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-253 | 25 | |
| α-helix | 259-261 | 3 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-348 | 61 | |
| α-helix | 357-366 | 10 | |
| α-helix | 536-558 | 23 | |
| α-helix | 564-599 | 36 | |
Chains E, F and H: 10 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| α-helix | 66-74 | 9 | |
| α-helix | 77-80 | 4 | |
| α-helix | 83-93 | 11 | |
| β-strand | 101 | 1 | 4 |
| α-helix | 103-110 | 8 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137 | 1 | 4 |
| α-helix | 139-147 | 9 | |
Chain G: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 71-85 | 15 | |
| α-helix | 91-114 | 24 | |
| α-helix | 119-147 | 29 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 196-210 | 15 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-253 | 25 | |
| α-helix | 259-261 | 3 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-348 | 61 | |
| α-helix | 357-366 | 10 | |
| α-helix | 536-558 | 23 | |
| α-helix | 564-599 | 36 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Potassium voltage-gated channel subfamily KQT member 2 | A, B, D, G | protein | 656 | Homo sapiens | O43526 (AlphaFold model) |
| Calmodulin-1 | C, E, F, H | protein | 177 | Homo sapiens | P0DP23 (AlphaFold model) |
Sequence of entity 1 (A, B, D, G), FASTA
>8J01_1 Potassium voltage-gated channel subfamily KQT member 2 (chains A, B, D, G)
MAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSS
EGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAV
LAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLC
LILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGV
SFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQY
YERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCR
GPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPK
SWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRA
VCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDK
DRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAK
EPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSVEGGSSGGWSHPQFEK
Sequence of entity 2 (C, E, F, H), FASTA
>8J01_2 Calmodulin-1 (chains C, E, F, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| P0T | cannabidiol | C21 H30 O2 | 8 |
| PIO | [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d… | C25 H49 O19 P3 | 4 |
Primary citation
Ligand activation mechanisms of human KCNQ2 channel. Ma, D., Zheng, Y., Li, X. et al. Nat Commun (2023) 14:6632-6632. DOI 10.1038/s41467-023-42416-x · PubMed
Other PDB entries of the same protein (UniProt O43526 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 22AY 2.3 Å, KCNQ2 homotetramer in apo state
- 22BJ 2.4 Å, KCNQ2/3 heterotetramer with 3:1 stoichiometry
- 22BF 2.5 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2
- 22BG 2.5 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3
- 8IZY 2.5 Å, Human KCNQ2-CaM in complex with HN37
- 22BE 2.6 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1
- 22BI 2.6 Å, XEN1101 bound KCNQ2/3 heteromer with 2:2 stoichiometry
- 22AZ 2.7 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1
- 22BK 2.7 Å, KCNQ2/3 heterotetramer with 2:2 stoichiometry
- 8J03 2.7 Å, Human KCNQ2(F104A)-CaM-PIP2-CBD complex in state I
- 8J04 2.7 Å, Human KCNQ2-CaM-HN37 complex in the presence of PIP2
- 8J05 2.7 Å, Human KCNQ2-CaM complex in the presence of PIP2
Browse structure collections
About this viewer
MolViewer shows 8J01 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.