6CZQ: PDB entry 6CZQ

A V-to-F substitution in SK2 channels causes Ca2+ hypersensitivity and improves locomotion in a C. elegans ALS model. Determined by X-ray diffraction at 2.2 Å resolution. Released 1 Aug 2018.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Rattus norvegicus
Chains: 2
Atoms: 2,087
Mol. weight: 28.12 kDa
Ligands: CA
Released: 1 Aug 2018

Explore 6CZQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CZQ contains 12 α-helices and 6 β-strands across 2 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 B: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	400-401	2	1
α-helix	402-404	3
α-helix	414-439	26
α-helix	446-485	40
α-helix	486-488	3

Chain R: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	2
α-helix	29-38	10
α-helix	45-55	11
β-strand	63-64	2	2
α-helix	65-73	9
β-strand	78-79	2	1
α-helix	82-90	9
β-strand	99-101	3	3
α-helix	102-111	10
α-helix	118-128	11
β-strand	135-137	3	3
α-helix	138-145	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Small conductance calcium-activated potassium channel protein 2	B	protein	95	Rattus norvegicus	P70604 (AlphaFold model)
Calmodulin-1	R	protein	146	Rattus norvegicus	P0DP29 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>6CZQ_1 Small conductance calcium-activated potassium channel protein 2 (chains B)
GRKLELTKAEKHFHNFMMDTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQR
KFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQLE

Sequence of entity 2 (R), FASTA

>6CZQ_2 Calmodulin-1 (chains R)
AALTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNG
TIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEV
DEMIREADIDGDGQVNYEEFVQMMTA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2

Water and common crystallization additives (SO4) are not listed.

Primary citation

A V-to-F substitution in SK2 channels causes Ca2+hypersensitivity and improves locomotion in a C. elegans ALS model. Nam, Y.W., Baskoylu, S.N., Gazgalis, D. et al. Sci Rep (2018) 8:10749-10749. DOI 10.1038/s41598-018-28783-2 · PubMed

Other PDB entries of the same protein (UniProt P70604 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4J9Y 1.51 Å, Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance…
1G4Y 1.6 Å, 1.60 a crystal structure of the gating domain from small conductance potassium channel…
4G28 1.63 Å, Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance…
4G27 1.65 Å, Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance…
4J9Z 1.66 Å, Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance…
3SJQ 1.9 Å, Crystal structure of a small conductance potassium channel splice variant complexed with…
4QNH 2.02 Å, Calcium-calmodulin (T79D) complexed with the calmodulin binding domain from a small…
2PNV 2.1 Å, Crystal Structure of the leucine zipper domain of small-conductance Ca2+-activated K+…
9O7S 2.71 Å, Cryo-EM structure of KCa2.2/calmodulin channel in complex with NS309
9O93 2.96 Å, Cryo-EM structure of KCa2.2_II/calmodulin channel in complex with rimtuzalcap
1QX7 3.09 Å, Crystal structure of apoCaM bound to the gating domain of small conductance…
8V2H 3.1 Å, Cryo-EM structure of the KCa2.2 channel bound to inhibitor AP14145.

Browse structure collections

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