9ZRL: KCa3.1_II/calmodulin channel

Cryo-EM structure of KCa3.1_II/calmodulin channel in complex with SKA111. Determined by electron microscopy at 3.38 Å resolution. Released 14 Jan 2026.

Method
Electron microscopy
Resolution
3.38 Å
Organism
Homo sapiens
Chains
8
Atoms
11,999
Mol. weight
185.82 kDa
Released
14 Jan 2026

Explore 9ZRL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9ZRL contains 82 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: 16 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix13-2311
α-helix29-4921
α-helix55-9137
α-helix102-11413
α-helix143-1464
α-helix149-1546
α-helix155-1617
α-helix163-1719
α-helix177-1859
α-helix192-20211
α-helix204-21310
α-helix219-2268
α-helix237-24812
α-helix263-28725
α-helix293-32634
α-helix334-36835
Chain B: 16 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix13-2513
α-helix28-4922
α-helix57-8731
α-helix103-11513
α-helix147-1548
α-helix155-1617
α-helix162-1709
α-helix172-1754
α-helix177-18610
α-helix194-2029
α-helix204-2074
α-helix209-22618
α-helix237-24812
α-helix263-28725
α-helix293-33038
α-helix335-36834
Chain C: 16 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix10-145
α-helix15-5036
α-helix60-8728
α-helix102-11413
α-helix147-1537
α-helix154-1629
α-helix163-1708
α-helix177-1848
α-helix185-1873
α-helix192-20211
α-helix204-2074
α-helix209-22618
α-helix237-24812
α-helix263-28725
α-helix293-32634
α-helix336-36833
Chain D: 18 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix13-2412
α-helix28-4922
α-helix55-8733
α-helix88-925
α-helix96-983
α-helix102-11514
α-helix144-1463
α-helix149-1546
α-helix155-1617
α-helix162-1709
α-helix177-18610
α-helix192-20211
α-helix204-2074
α-helix209-22618
α-helix237-24812
α-helix263-28725
α-helix293-33038
α-helix334-36835
Chain E: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix88-914
β-strand10011
α-helix102-1098
α-helix121-1277
β-strand13611
α-helix139-1435
Chain F: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix88-914
β-strand10012
α-helix102-1109
α-helix118-12710
β-strand13612
α-helix139-1468
Chain G: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix88-914
β-strand100-10123
α-helix102-1109
α-helix118-1269
β-strand135-13623
α-helix139-1468
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix88-914
β-strand10014
α-helix102-1109
α-helix118-12811
β-strand13614
α-helix139-1468

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Intermediate conductance calcium-activated potassium channel protein 4A, B, C, Dprotein343Homo sapiensO15554 (AlphaFold model)
Calmodulin-1E, F, G, Hprotein67Homo sapiensP0DP23 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9ZRL_1 Intermediate conductance calcium-activated potassium channel protein 4 (chains A, B, C, D)
LGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISIS
TFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRPGFLG
QGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGR
LLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIV
CLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQEAWMFY
KHTRRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMV
Sequence of entity 2 (E, F, G, H), FASTA
>9ZRL_2 Calmodulin-1 (chains E, F, G, H)
SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEE
FVQMMTA

Primary citation

Structural basis for the subtype-selective activation of K Ca 3.1 channels. Ramanishka, A., Nasburg, J.A., Xu, Y. et al. Structure (2026) 34:1040-1049.e3. DOI 10.1016/j.str.2026.04.010 · PubMed

Other PDB entries of the same protein (UniProt O15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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