8U30: TRPV1 in nanodisc

TRPV1 in nanodisc bound with diC8-PIP2 in the closed state. Determined by electron microscopy at 3.0 Å resolution. Released 8 May 2024.

Method
Electron microscopy
Resolution
3.0 Å
Organism
Rattus norvegicus
Chains
4
Atoms
17,309
Mol. weight
373.63 kDa
Ligands
PIO
Released
8 May 2024

Explore 8U30 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8U30 contains 128 α-helices and 20 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: 32 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix204-2118
α-helix214-22310
α-helix234-2363
α-helix251-2566
α-helix261-2688
α-helix274-2763
α-helix287-2948
α-helix299-31921
α-helix325-3273
α-helix336-3438
α-helix346-3538
α-helix363-3653
β-strand368-37471
β-strand377-38371
α-helix395-4006
α-helix411-4144
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix469-49931
α-helix505-5073
α-helix511-53121
α-helix537-55115
α-helix552-5565
α-helix560-57213
α-helix573-5775
α-helix578-59821
α-helix603-6283
α-helix630-63910
α-helix640-6423
α-helix656-66712
α-helix668-6747
α-helix675-68814
α-helix690-71122
β-strand72612
β-strand73812
β-strand741-74771

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily V member 1A, B, C, Dprotein815Rattus norvegicusO35433 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>8U30_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D)
MEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASP
LDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRSIFDA
VAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDVA
RKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFFKKTK
GRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTVD
NTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEP
ECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNR
LLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEIL
SVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVAS
MVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIE
DGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMG
ETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDYRWCFR
VDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRD
RHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPGEK

Ligands and cofactors

IDNameFormulaCopies
PIO[(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d…C25 H49 O19 P34

Water and common crystallization additives (NA) are not listed.

Primary citation

Structural basis of TRPV1 modulation by endogenous bioactive lipids. Arnold, W.R., Mancino, A., Moss 3rd, F.R. et al. Nat Struct Mol Biol (2024) 31:1377-1385. DOI 10.1038/s41594-024-01299-2 · PubMed

Other PDB entries of the same protein (UniProt O35433 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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