8J03: PDB entry 8J03
Human KCNQ2(F104A)-CaM-PIP2-CBD complex in state I. Determined by electron microscopy at 2.7 Å resolution. Released 6 Dec 2023.
- Method
- Electron microscopy
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 15,232
- Mol. weight
- 373.93 kDa
- Ligands
- P0T
- Released
- 6 Dec 2023
Explore 8J03 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8J03 contains 90 α-helices and 16 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.
Chains A and D: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 71-85 | 15 | |
| α-helix | 92-113 | 22 | |
| α-helix | 119-147 | 29 | |
| α-helix | 148-150 | 3 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 197-209 | 13 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-254 | 26 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-326 | 39 | |
| α-helix | 333-347 | 15 | |
| α-helix | 536-559 | 24 | |
| α-helix | 565-594 | 30 | |
Chain E: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 28 | 1 | 1 |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64 | 1 | 1 |
| α-helix | 66-74 | 9 | |
| α-helix | 83-93 | 11 | |
| β-strand | 100-101 | 2 | 2 |
| α-helix | 103-110 | 8 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137-138 | 2 | 2 |
| α-helix | 140-147 | 8 | |
Chains F and H: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 28 | 1 | 7 |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64 | 1 | 7 |
| α-helix | 66-73 | 8 | |
| α-helix | 83-93 | 11 | |
| β-strand | 100-101 | 2 | 8 |
| α-helix | 103-110 | 8 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137-138 | 2 | 8 |
| α-helix | 140-147 | 8 | |
Chains G and I: 15 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 71-85 | 15 | |
| α-helix | 92-113 | 22 | |
| α-helix | 119-147 | 29 | |
| α-helix | 148-150 | 3 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 197-209 | 13 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-254 | 26 | |
| α-helix | 259-261 | 3 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-326 | 39 | |
| α-helix | 333-347 | 15 | |
| α-helix | 536-559 | 24 | |
| α-helix | 565-594 | 30 | |
Chain J: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 28 | 1 | 5 |
| α-helix | 30-39 | 10 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64 | 1 | 5 |
| α-helix | 66-73 | 8 | |
| α-helix | 83-93 | 11 | |
| β-strand | 100-101 | 2 | 6 |
| α-helix | 103-110 | 8 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137-138 | 2 | 6 |
| α-helix | 140-147 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Potassium voltage-gated channel subfamily KQT member 2 | A, D, G, I | protein | 656 | Homo sapiens | O43526 (AlphaFold model) |
| Calmodulin-1 | E, F, H, J | protein | 177 | Homo sapiens | P0DP23 (AlphaFold model) |
Sequence of entity 1 (A, D, G, I), FASTA
>8J03_1 Potassium voltage-gated channel subfamily KQT member 2 (chains A, D, G, I)
MAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVASCLVLSVFSTIKEYEKSS
EGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAV
LAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLC
LILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGV
SFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQY
YERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCR
GPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPK
SWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRA
VCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDK
DRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAK
EPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSVEGGSSGGWSHPQFEK
Sequence of entity 2 (E, F, H, J), FASTA
>8J03_2 Calmodulin-1 (chains E, F, H, J)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| P0T | cannabidiol | C21 H30 O2 | 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
- 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
- 22BC 2.8 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3
Browse structure collections
About this viewer
MolViewer shows 8J03 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.