6O1U: TRPV5 W583A in nanodisc

Cryo-EM structure of TRPV5 W583A in nanodisc. Determined by electron microscopy at 2.8 Å resolution. Released 24 Apr 2019.

Method: Electron microscopy
Resolution: 2.8 Å
Organism: Oryctolagus cuniculus
Chains: 4
Atoms: 19,612
Mol. weight: 331.14 kDa
Released: 24 Apr 2019

Explore 6O1U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6O1U contains 160 α-helices and 44 β-strands across 4 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.

Chains A, B, C and D: 40 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	29-46	18
α-helix	48-55	8
α-helix	58-66	9
α-helix	82-88	7
α-helix	92-101	10
α-helix	103-105	3
α-helix	108-110	3
α-helix	113-115	3
α-helix	120-126	7
α-helix	130-138	9
α-helix	166-172	7
α-helix	176-182	7
α-helix	199-204	6
α-helix	209-221	13
α-helix	243-249	7
α-helix	253-259	7
β-strand	264-270	7	1
β-strand	273-278	6	1
α-helix	281-284	4
α-helix	292-297	6
α-helix	303-309	7
α-helix	313-320	8
α-helix	321-325	5
α-helix	326-348	23
β-strand	352-354	3	2
β-strand	366	1	3
β-strand	368	1	4
β-strand	370-372	3	2
α-helix	380-410	31
α-helix	414-417	4
α-helix	426-445	20
α-helix	451-463	13
α-helix	464-471	8
α-helix	476-484	9
α-helix	485-489	5
α-helix	494-498	5
α-helix	500-511	12
β-strand	515	1	5
α-helix	521-523	3
α-helix	526-538	13
α-helix	542-544	3
β-strand	550	1	6
α-helix	553-562	10
α-helix	563-570	8
α-helix	571-583	13
α-helix	598-607	10
α-helix	614-616	3
β-strand	618-619	2	7
α-helix	628	1
β-strand	629-630	2	7
β-strand	631-636	6	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transient receptor potential cation channel subfamily V member 5	A, B, C, D	protein	730	Oryctolagus cuniculus	Q9XSM3 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6O1U_1 Transient receptor potential cation channel subfamily V member 5 (chains A, B, C, D)
MGACPPKAKGPWAQLQKLLISWPVGEQDWEQYRDRVNMLQQERIRDSPLLQAAKENDLRL
LKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPELAKEPALCEPFVGQTA
LHIAVMNQNLNLVRALLARGASVSARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVR
LLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDEHSDHLQSLELVPNHQG
LTPFKLAGVEGNTVMFQHLMQKRKHVQWTCGPLTSTLYDLTEIDSWGEELSFLELVVSSK
KREARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCCIYRPLKLRDDNRT
DPRDITILQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTI
LGGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTI
MIQKMIFGDLMRFCWLMAVVILGFASAFHITFQTEDPNNLGEFSDYPTALFSTFELFLTI
IDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHARVAQERDELWRAQVVAT
TVMLERKMPRFLWPRSGICGYEYGLGDRWFLRVENHHDQNPLRVLRYVEAFKCSDKEDGQ
EQLSEKRPSTVESGMLSRASVAFQTPSLSRTTSQSSNSHRGWEILRRNTLGHLNLGLDLG
EGDGEEVYHF

Primary citation

Structural insight into TRPV5 channel function and modulation. Dang, S., van Goor, M.K., Asarnow, D. et al. Proc Natl Acad Sci U S A (2019) 116:8869-8878. DOI 10.1073/pnas.1820323116 · PubMed

Other PDB entries of the same protein (UniProt Q9XSM3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8TF2 2.57 Å, Wildtype rabbit TRPV5 into nanodiscs in Apo state
7T6O 2.6 Å, Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 3
8FFQ 2.65 Å, Wildtype rabbit TRPV5 into nanodiscs in the presence of PI(4,5)P2 and ruthenium red
7T6M 2.8 Å, Cryo-EM structure of TRPV5 in nanodiscs with PI(4,5)P2 at pH6 state 1
7T6P 2.8 Å, Cryo-EM structure of TRPV5 T709D in nanodiscs
8TF4 2.86 Å, Wildtype rabbit TRPV5 into nanodiscs in the presence of PI(4,5)P2 and econazole
6O1N 2.9 Å, Cryo-EM structure of TRPV5 (1-660) in nanodisc
7T6N 2.9 Å, Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 2
8TF3 2.94 Å, Wildtype rabbit TRPV5 into nanodiscs in complex with econazole
8FFN 2.96 Å, RR-bound wildtype rabbit TRPV5 in nanodiscs
6O1P 3.0 Å, Cryo-EM structure of full length TRPV5 in nanodisc
7T6K 3.0 Å, Cryo-EM structure of TRPV5 at pH6 in nanodiscs

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