9Y5Q: PDB entry 9Y5Q

Cryo EM structure of KCa3.1_R355K_I/calmodulin channel in complex with rimtuzalcap. Determined by electron microscopy at 4.73 Å resolution. Released 15 Oct 2025.

Method
Electron microscopy
Resolution
4.73 Å
Organism
Homo sapiens
Chains
8
Atoms
15,135
Mol. weight
238.08 kDa
Ligands
CA, A1B92
Released
15 Oct 2025

Explore 9Y5Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Y5Q contains 100 α-helices and 0 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-helix10-4940
α-helix58-9134
α-helix96-994
α-helix102-11615
α-helix151-1555
α-helix156-1583
α-helix162-1709
α-helix177-1848
α-helix194-2029
α-helix204-22320
α-helix243-2486
α-helix261-27818
α-helix283-2886
α-helix293-33038
α-helix336-36631
α-helix370-38415
Chain B: 18 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix10-4334
α-helix52-543
α-helix57-9034
α-helix96-994
α-helix102-11615
α-helix151-1544
α-helix155-1617
α-helix162-1698
α-helix177-1837
α-helix194-2029
α-helix206-22318
α-helix237-2404
α-helix243-2486
α-helix263-27816
α-helix282-2898
α-helix293-33038
α-helix335-36632
α-helix370-38415
Chain C: 18 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix10-3930
α-helix43-486
α-helix55-9036
α-helix102-11615
α-helix151-1544
α-helix155-1617
α-helix162-1709
α-helix172-1743
α-helix177-1848
α-helix194-2029
α-helix206-22621
α-helix237-2404
α-helix261-27717
α-helix282-2887
α-helix293-33038
α-helix335-3373
α-helix338-36831
α-helix371-38414
Chain D: 16 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix10-4839
α-helix57-9034
α-helix104-11613
α-helix147-1548
α-helix155-1617
α-helix162-1709
α-helix177-1848
α-helix194-2029
α-helix208-22417
α-helix237-24812
α-helix261-27818
α-helix282-2854
α-helix293-33038
α-helix335-34713
α-helix350-36718
α-helix371-38414
Chains E and G: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-1914
α-helix29-3810
α-helix45-5511
α-helix65-739
α-helix85-895
α-helix102-1098
α-helix120-1289
α-helix138-1458
Chain F: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-1914
α-helix29-3911
α-helix45-5511
α-helix65-739
α-helix87-904
α-helix102-1098
α-helix120-1289
α-helix138-1458
Chain H: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-1914
α-helix29-3810
α-helix45-5511
α-helix65-739
α-helix85-895
α-helix102-1098
α-helix120-1289
α-helix138-1469

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Intermediate conductance calcium-activated potassium channel protein 4A, B, C, Dprotein378Homo sapiensO15554 (AlphaFold model)
Calmodulin-1E, F, G, Hprotein146Homo sapiensP0DP23 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9Y5Q_1 Intermediate conductance calcium-activated potassium channel protein 4 (chains A, B, C, D)
LGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISIS
TFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCV
QDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQV
RFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITF
LTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYT
KEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVKLKHRKLREQVNSM
VDISKMHMILYDLQQNLS
Sequence of entity 2 (E, F, G, H), FASTA
>9Y5Q_2 Calmodulin-1 (chains E, F, G, H)
DQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNG
TIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEV
DEMIREADIDGDGQVNYEEFVQMMTA

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4
A1B92RimtuzalcapC18 H24 F2 N6 O4

Water and common crystallization additives (K) are not listed.

Primary citation

Structural basis for the subtype-selectivity of K Ca 2.2 channel activators. Nam, Y.W., Ramanishka, A., Xu, Y. et al. Nat Commun (2026) 17:531-531. DOI 10.1038/s41467-025-67232-3 · 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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