6ALE: PDB entry 6ALE

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 2.5 Å resolution. Released 8 Aug 2018.

Method: X-ray diffraction
Resolution: 2.5 Å
Organisms: Homo sapiens, Rattus norvegicus
Chains: 2
Atoms: 2,096
Mol. weight: 28.54 kDa
Ligands: CA, 1KP
Released: 8 Aug 2018

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

Secondary structure: helices and β-sheets

6ALE 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	402-403	2
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	102-109	8
α-helix	118-128	11
β-strand	135-137	3	3
α-helix	138-146	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Small conductance calcium-activated potassium channel protein 2	B	protein	95	Homo sapiens	Q9H2S1 (AlphaFold model)
Calmodulin-2	R	protein	146	Rattus norvegicus	P0DP30 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>6ALE_1 Small conductance calcium-activated potassium channel protein 2 (chains B)
GRKLELTKAEKHFHNFMMDTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQR
KFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQLE

Sequence of entity 2 (R), FASTA

>6ALE_2 Calmodulin-2 (chains R)
AALTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNG
TIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEV
DEMIREADIDGDGQVNYEEFVQMMTA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
1KP	(3E)-6,7-dichloro-3-(hydroxyimino)-1,3-dihydro-2H-indol-2-one	C8 H4 Cl2 N2 O2	1

Water and common crystallization additives (GOL, 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 Q9H2S1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5V03 1.58 Å, A positive allosteric modulator binding pocket in SK2 ion channels is shared by Riluzole…
5V02 1.78 Å, A positive allosteric modulator binding pocket in SK2 ion channels is shared by Riluzole…
5WBX 1.9 Å, Structural insights into the potency of SK/IK channel positive modulators
5WC5 2.3 Å, Structural insights into the potency of SK/IK channel positive modulators
9ZRQ 2.77 Å, Cryo-EM structure of KCa2.2/calmodulin channel in complex with SKA31.
9VUC 2.96 Å, channel B complex with 2
9O48 3.1 Å, Cryo-EM structure of the human SK2-4 chimera/calmodulin channel complex in the Ca2+…
9O5O 3.1 Å, Cryo-EM structure of the human SK2-4 chimera/calmodulin channel complex bound to a small…
9O52 3.18 Å, Cryo-EM structure of the human SK2-4 chimera/calmodulin channel complex bound to the bee…
9VUA 3.23 Å, channel A complex with 1
9O53 3.3 Å, Cryo-EM structure of the human SK2-4 chimera/calmodulin channel complex bound to a small…
9ZRR 3.31 Å, Cryo-EM structure of KCa2.2/calmodulin channel in complex with SKA111.

Browse structure collections

About this viewer

MolViewer shows 6ALE directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.