8J00: Human KCNQ2-CaM
Human KCNQ2-CaM in complex with CBD. Determined by electron microscopy at 3.0 Å resolution. Released 29 Nov 2023.
- Method
- Electron microscopy
- Resolution
- 3.0 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 15,240
- Mol. weight
- 375.49 kDa
- Ligands
- P0T
- Released
- 29 Nov 2023
Explore 8J00 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8J00 contains 91 α-helices and 10 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, B, C and D: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 71-85 | 15 | |
| α-helix | 92-114 | 23 | |
| α-helix | 119-147 | 29 | |
| α-helix | 148-150 | 3 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 197-210 | 14 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-254 | 26 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-326 | 39 | |
| α-helix | 334-349 | 16 | |
| α-helix | 542-559 | 18 | |
| α-helix | 564-594 | 31 | |
Chain E: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| α-helix | 30-40 | 11 | |
| α-helix | 43-45 | 3 | |
| α-helix | 46-56 | 11 | |
| α-helix | 66-74 | 9 | |
| α-helix | 83-93 | 11 | |
| β-strand | 100-102 | 3 | 1 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 1 |
| α-helix | 141-147 | 7 | |
Chain F: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| α-helix | 30-40 | 11 | |
| α-helix | 43-45 | 3 | |
| α-helix | 46-56 | 11 | |
| α-helix | 66-74 | 9 | |
| α-helix | 83-93 | 11 | |
| β-strand | 100-102 | 3 | 2 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 2 |
| α-helix | 140-147 | 8 | |
Chain G: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 28 | 1 | 3 |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64 | 1 | 3 |
| α-helix | 66-73 | 8 | |
| α-helix | 83-93 | 11 | |
| β-strand | 100-102 | 3 | 4 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 4 |
| α-helix | 141-147 | 7 | |
Chain H: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| α-helix | 30-40 | 11 | |
| α-helix | 42-45 | 4 | |
| α-helix | 46-56 | 11 | |
| α-helix | 66-73 | 8 | |
| α-helix | 83-93 | 11 | |
| β-strand | 100-102 | 3 | 5 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 5 |
| α-helix | 140-147 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Potassium voltage-gated channel subfamily KQT member 2 | A, B, C, D | protein | 656 | Homo sapiens | O43526 (AlphaFold model) |
| Calmodulin-1 | E, F, G, H | protein | 177 | Homo sapiens | P0DP23 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>8J00_1 Potassium voltage-gated channel subfamily KQT member 2 (chains A, B, C, D)
MAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSS
EGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAV
LAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLC
LILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGV
SFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQY
YERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCR
GPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPK
SWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRA
VCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDK
DRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAK
EPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSVEGGSSGGWSHPQFEK
Sequence of entity 2 (E, F, G, H), FASTA
>8J00_2 Calmodulin-1 (chains E, F, G, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| P0T | cannabidiol | C21 H30 O2 | 8 |
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
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