2L0W: N-terminal PAS domain of HERG potassium channel

Solution NMR structure of the N-terminal PAS domain of HERG potassium channel. Determined by solution NMR. Released 26 Jan 2011.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 1,067
Mol. weight: 15.5 kDa
Released: 26 Jan 2011

Explore 2L0W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2L0W contains 6 α-helices and 7 β-strands across 1 chain. 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: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	9-12	4
α-helix	14-22	9
β-strand	28-33	6	1
β-strand	40	1	2
β-strand	41-44	4	1
α-helix	47-52	6
α-helix	56-59	4
β-strand	63	1	2
α-helix	67-69	3
α-helix	76-85	10
β-strand	92-99	8	1
β-strand	105-116	12	1
β-strand	122-134	13	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel, subfamily H (Eag-related), member 2, isoform CRA_b	A	protein	138	Homo sapiens	Q12809 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2L0W_1 Potassium voltage-gated channel, subfamily H (Eag-related), member 2, isoform CRA_b (chains A)
GGSMPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRA
EVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKN
EDGAVIMFILNFEVVMEK

Primary citation

The N-Terminal Tail of hERG Contains an Amphipathic alpha-Helix That Regulates Channel Deactivation. Ng, C.A., Hunter, M.J., Perry, M.D. et al. PLoS One (2011) 6:e16191-e16191. DOI 10.1371/journal.pone.0016191 · PubMed

Other PDB entries of the same protein (UniProt Q12809 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4HQA 1.96 Å, Crystal structure of PAS domain from the human ERG (hERG) potassium channel
4HP9 2.12 Å, Crystal structure of the N-terminal truncated PAS domain from the hERG potassium channel
1BYW 2.6 Å, Structure of the N-terminal domain of the human-erg potassium channel
9CHQ 3.0 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 3 mM K+
8ZYQ 3.18 Å, Cryo-EM Structure of pimozide-bound hERG Channel
8ZYP 3.19 Å, Cryo-EM Structure of E-4031-bound hERG Channel
8ZYN 3.27 Å, Cryo-EM Structure of inhibitor-free hERG Channel
8ZYO 3.29 Å, Cryo-EM Structure of astemizole-bound hERG Channel
9CHP 3.3 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 300 mM K+
9CHS 3.4 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 3 mM K+…
8IO4 3.5 Å, Herg1a-herg1b open state
9CHR 3.5 Å, Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 300 mM K+…

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