5VA1: Human ether-a-go-go related K+ channel

Cryo-EM structure of the human ether-a-go-go related K+ channel. Determined by electron microscopy at 3.7 Å resolution. Released 3 May 2017.

Method: Electron microscopy
Resolution: 3.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 4,407
Mol. weight: 88.9 kDa
Released: 3 May 2017

Explore 5VA1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5VA1 contains 27 α-helices and 22 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: 27 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
α-helix	14-25	12
β-strand	28-33	6	1
β-strand	40	1	2
β-strand	41-44	4	1
α-helix	46-52	7
α-helix	56-59	4
β-strand	63	1	2
α-helix	76-88	13
β-strand	92-99	8	1
β-strand	105-116	12	1
β-strand	122-130	9	1
β-strand	400	1	3
α-helix	405-430	26
α-helix	451-472	22
β-strand	473	1	3
β-strand	475	1	4
β-strand	483	1	4
α-helix	486-493	8
α-helix	498-504	7
α-helix	523-532	10
α-helix	533-537	5
α-helix	539-542	4
α-helix	546-574	29
α-helix	585-592	8
α-helix	607-622	16
α-helix	635-666	32
α-helix	669-687	19
α-helix	691-708	18
α-helix	713-717	5
α-helix	722-732	11
α-helix	734-739	6
α-helix	748-757	10
β-strand	759-763	5	5
β-strand	768-770	3	6
β-strand	775	1	7
β-strand	780-782	3	5
β-strand	787-790	4	6
β-strand	795-799	5	6
β-strand	803-806	4	5
α-helix	809-812	4
α-helix	816	1
β-strand	817	1	7
α-helix	818	1
β-strand	821-824	4	6
β-strand	828-832	5	5
α-helix	835-844	10
α-helix	846-855	10
β-strand	860-861	2	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily H member 2	A	protein	795	Homo sapiens	Q12809 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5VA1_1 Potassium voltage-gated channel subfamily H member 2 (chains A)
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVM
QRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG
AVIMFILNFEVVMEKDMVGSGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIY
TAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANE
EVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLD
RYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSS
GLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVS
AIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGF
PECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALY
FISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLE
VLDMYPEFSDHFWSSLEITFNLRDTNMIPGGRQYQELPRCPAPTPSLLNIPLSSPGRRPR
GDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSTSPLL
PVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPGQLGALTSQPLHRHGS
DPGSEASNSLEVLFQ

Primary citation

Cryo-EM Structure of the Open Human Ether-a-go-go-Related K(+) Channel hERG. Wang, W., MacKinnon, R. Cell (2017) 169:422-430.e10. DOI 10.1016/j.cell.2017.03.048 · 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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