5IRX: TRPV1

Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc. Determined by electron microscopy at 2.95 Å resolution. Released 25 May 2016.

Method
Electron microscopy
Resolution
2.95 Å
Organisms
Rattus norvegicus, Haplopelma schmidti
Chains
6
Atoms
13,162
Mol. weight
317.88 kDa
Ligands
6O9, 6EU, 6OE, 6O8
Released
25 May 2016

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

Secondary structure: helices and β-sheets

5IRX contains 94 α-helices and 60 β-strands across 6 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: 22 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix336-3416
α-helix346-3538
β-strand369-37461
β-strand377-38151
α-helix395-4006
α-helix412-4154
α-helix419-4257
α-helix426-4305
α-helix431-45323
α-helix462-4632
α-helix469-49830
α-helix511-53121
α-helix537-55014
α-helix551-5544
β-strand55712
β-strand55912
α-helix564-5718
α-helix572-5776
α-helix578-5803
α-helix584-59815
α-helix630-64112
α-helix656-66712
α-helix668-6747
α-helix675-69117
α-helix693-71220
α-helix716-7194
β-strand724-72523
β-strand739-74023
β-strand743-74641
Chains E and F: 3 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand3113
β-strand5114
β-strand7114
β-strand8115
β-strand15113
β-strand22116
β-strand30115
β-strand32116
α-helix33-364
β-strand45117
β-strand50118
β-strand51119
β-strand55119
β-strand57117
β-strand62120
α-helix691
β-strand70118
α-helix711
β-strand72120

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily V member 1A, B, C, Dprotein636Rattus norvegicusO35433 (AlphaFold model)
Tau-theraphotoxin-Hs1aE, Fprotein75Haplopelma schmidtiP0CH43 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5IRX_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D)
AMGSRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNL
HNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGA
DVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGN
TVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGK
IGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSE
TPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKL
KNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLV
SVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYL
VFLFGFSTAVVTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVI
LTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQV
GFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPG
Sequence of entity 2 (E, F), FASTA
>5IRX_2 Tau-theraphotoxin-Hs1a (chains E, F)
DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPVTTNCAKEGEVCGWGSKCCHG
LDCPLAFIPYCEKYR

Ligands and cofactors

IDNameFormulaCopies
6O9(2S)-2-(acetyloxy)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}propyl…C12 H24 N O8 P4
6EUresiniferatoxinC37 H40 O94
6OE(2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl…C17 H34 N O8 P8
6O8(4R,7S)-4-hydroxy-N,N,N-trimethyl-4,9-dioxo-7-[(pentanoyloxy)methyl]-3,5,8-trio…C19 H39 N O8 P4

Primary citation

TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. Gao, Y., Cao, E., Julius, D. et al. Nature (2016) 534:347-351. DOI 10.1038/nature17964 · PubMed

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

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