22RJ: Human KCNQ3-CaM in apo state
Human KCNQ3-CaM in apo state. Determined by electron microscopy at 2.82 Å resolution. Released 3 Jun 2026.
- Method
- Electron microscopy
- Resolution
- 2.82 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 14,952
- Mol. weight
- 455.03 kDa
- Released
- 3 Jun 2026
Explore 22RJ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
22RJ contains 100 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.
Chain A: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 104-115 | 12 | |
| α-helix | 125-142 | 18 | |
| α-helix | 151-178 | 28 | |
| α-helix | 182-184 | 3 | |
| α-helix | 187-193 | 7 | |
| α-helix | 197-209 | 13 | |
| α-helix | 212-215 | 4 | |
| α-helix | 228-238 | 11 | |
| α-helix | 245-256 | 12 | |
| α-helix | 258-283 | 26 | |
| α-helix | 303-314 | 12 | |
| α-helix | 327-364 | 38 | |
| α-helix | 373-387 | 15 | |
| α-helix | 517-536 | 20 | |
| α-helix | 540-541 | 2 | |
| α-helix | 543-572 | 30 | |
Chains B and C: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 104-115 | 12 | |
| α-helix | 125-142 | 18 | |
| α-helix | 151-178 | 28 | |
| α-helix | 182-184 | 3 | |
| α-helix | 187-193 | 7 | |
| α-helix | 197-209 | 13 | |
| α-helix | 212-215 | 4 | |
| α-helix | 228-238 | 11 | |
| α-helix | 245-256 | 12 | |
| α-helix | 258-283 | 26 | |
| α-helix | 303-314 | 12 | |
| α-helix | 327-364 | 38 | |
| α-helix | 373-387 | 15 | |
| α-helix | 517-538 | 22 | |
| α-helix | 540-541 | 2 | |
| α-helix | 543-572 | 30 | |
Chain D: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 104-115 | 12 | |
| α-helix | 125-142 | 18 | |
| α-helix | 151-178 | 28 | |
| α-helix | 182-184 | 3 | |
| α-helix | 187-193 | 7 | |
| α-helix | 197-209 | 13 | |
| α-helix | 212-215 | 4 | |
| α-helix | 228-238 | 11 | |
| α-helix | 245-256 | 12 | |
| α-helix | 258-283 | 26 | |
| α-helix | 303-314 | 12 | |
| α-helix | 327-364 | 38 | |
| α-helix | 372-387 | 16 | |
| α-helix | 517-536 | 20 | |
| α-helix | 540-541 | 2 | |
| α-helix | 543-572 | 30 | |
Chain E: 9 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 27-28 | 2 | 1 |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 66-73 | 8 | |
| α-helix | 77-79 | 3 | |
| α-helix | 83-91 | 9 | |
| β-strand | 100-102 | 3 | 2 |
| α-helix | 103-110 | 8 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 2 |
| α-helix | 139-146 | 8 | |
Chains F and G: 9 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 27-28 | 2 | 3 |
| α-helix | 30-38 | 9 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 66-73 | 8 | |
| α-helix | 77-79 | 3 | |
| α-helix | 83-91 | 9 | |
| β-strand | 100-102 | 3 | 4 |
| α-helix | 103-110 | 8 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 4 |
| α-helix | 139-146 | 8 | |
Chain H: 9 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| β-strand | 27-28 | 2 | 7 |
| α-helix | 30-36 | 7 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64-65 | 2 | 7 |
| α-helix | 66-73 | 8 | |
| α-helix | 77-80 | 4 | |
| α-helix | 83-91 | 9 | |
| β-strand | 100-102 | 3 | 8 |
| α-helix | 103-110 | 8 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-138 | 3 | 8 |
| α-helix | 139-144 | 6 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Potassium voltage-gated channel subfamily KQT member 3 | A, B, C, D | protein | 872 | Homo sapiens | O43525 (AlphaFold model) |
| Calmodulin-1 | E, F, G, H | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>22RJ_1 Potassium voltage-gated channel subfamily KQT member 3 (chains A, B, C, D)
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAG
ADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRG
WALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGC
CCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRM
DRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEF
ETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQ
EQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAAS
SQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKA
YAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRP
YDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPR
NEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPT
KGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNL
PRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRR
SITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDT
DTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI
Sequence of entity 2 (E, F, G, H), FASTA
>22RJ_2 Calmodulin-1 (chains E, F, G, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK
Primary citation
Human KCNQ3-CaM in apo state. Cheng, X.Y., Wan, S.Y., Jiang, D.X. et al. To be published.
Other PDB entries of the same protein (UniProt O43525 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5J03 2.0 Å, Crystal Structure of a chimeric Kv7.2 - Kv7.3 proximal C-terminal Domain in Complex with…
- 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
- 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
- 22BC 2.8 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3
- 22BH 2.8 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 4
- 22BA 2.9 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2
- 22RQ 2.9 Å, Human KCNQ3-XEN1101 complex in the presence of PIP2
Browse structure collections
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