6MHS: PDB entry 6MHS

Structure of the human TRPV3 channel in a putative sensitized conformation. Determined by electron microscopy at 3.2 Å resolution. Released 3 Oct 2018.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 17,792
Mol. weight: 379.44 kDa
Released: 3 Oct 2018

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

Secondary structure: helices and β-sheets

6MHS contains 144 α-helices and 32 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: 36 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	119-129	11
α-helix	134-145	12
α-helix	146-148	3
α-helix	155-162	8
β-strand	163	1	7
β-strand	170	1	7
α-helix	171-177	7
α-helix	183-196	14
α-helix	200-204	5
β-strand	207	1	8
β-strand	217	1	8
α-helix	218-224	7
α-helix	228-236	9
α-helix	265-271	7
α-helix	275-283	9
α-helix	299-306	8
α-helix	310-313	4
α-helix	317-327	11
α-helix	332-335	4
α-helix	344-350	7
α-helix	355-361	7
α-helix	371-373	3
β-strand	376-382	7	9
β-strand	385-391	7	9
α-helix	403-409	7
α-helix	416-419	4
α-helix	423-432	10
α-helix	433-437	5
α-helix	438-460	23
α-helix	481-504	24
α-helix	521-541	21
α-helix	547-561	15
α-helix	562-568	7
α-helix	570-582	13
α-helix	583-587	5
α-helix	588-608	21
α-helix	625-637	13
α-helix	644-645	2
α-helix	651-662	12
α-helix	663-670	8
α-helix	671-705	35
α-helix	709-715	7
β-strand	719-722	4	9
β-strand	728-737	10	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transient receptor potential cation channel subfamily V member 3	A, B, C, D	protein	826	Homo sapiens	Q8NET8 (AlphaFold model)

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

>6MHS_1 Transient receptor potential cation channel subfamily V member 3 (chains A, B, C, D)
MEKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKT
SPPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRL
KKRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNI
NPNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGA
DVNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNI
LHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKY
ILSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEM
LTLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKM
GWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFL
YLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLL
GFGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLI
TYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGE
LCKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAF
EEVEEFPETSVVDAGLEVLFQGPAAAVDYKDDDDKAHHHHHHHHHH

Primary citation

Conformational ensemble of the human TRPV3 ion channel. Zubcevic, L., Herzik Jr., M.A., Wu, M. et al. Nat Commun (2018) 9:4773-4773. DOI 10.1038/s41467-018-07117-w · PubMed

Other PDB entries of the same protein (UniProt Q8NET8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6H9J 1.83 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPV3 (229-255)
6HA6 1.98 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPV3 (220-246)
7QQN 2.45 Å, The PDZ domain of SNTG1 complexed with the acetylated PDZ-binding motif of TRPV3
8V6K 2.46 Å, Apo-state cryo-EM structure of human TRPV3 in cNW30 nanodiscs
13LU 2.49 Å, Structure of human TRPV3-W521S Olmsted syndrome mutant in the closed state
7XJ0 2.53 Å, Structure of human TRPV3 in complex with Trpvicin
8GKA 2.55 Å, Human TRPV3 tetramer structure, closed conformation
8V6N 2.59 Å, Open-state cryo-EM structure of human TRPV3 in presence of 2-APB in cNW30 nanodiscs
9PJ5 2.76 Å, Closed-state structure of wild-type human TRPV3 purified in GDN detergent
8V6O 2.83 Å, Inactivated-state cryo-EM structure of human TRPV3 in presence of 2-APB in cNW30 nanodiscs
13LJ 2.86 Å, Structure of human TRPV3-G568C Olmsted syndrome mutant in the closed state
7XJ1 2.93 Å, Structure of human TRPV3_G573S in complex with Trpvicin in C2 symmetry

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