7L2H: Unliganded full-length TRPV1 at neutral pH

Cryo-EM structure of unliganded full-length TRPV1 at neutral pH. Determined by electron microscopy at 2.63 Å resolution. Released 22 Sept 2021.

Method
Electron microscopy
Resolution
2.63 Å
Organism
Rattus norvegicus
Chains
4
Atoms
17,556
Mol. weight
385.83 kDa
Ligands
XJ7, XJD
Released
22 Sept 2021

Explore 7L2H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7L2H contains 116 α-helices and 26 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.

Chain A: 28 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix204-2107
α-helix214-2229
α-helix251-2577
α-helix261-2699
α-helix287-2937
α-helix299-31921
α-helix336-3427
α-helix346-3538
α-helix363-3653
β-strand368-37361
β-strand377-38371
α-helix395-4006
α-helix412-4143
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix463-4664
α-helix469-49931
α-helix505-5084
α-helix511-53121
α-helix537-55014
α-helix551-5566
α-helix560-57213
α-helix573-5775
α-helix578-59821
α-helix630-64112
α-helix656-66611
α-helix667-6759
α-helix676-68712
α-helix690-71122
β-strand726-73052
β-strand736-73832
β-strand741-74771
Chain B: 30 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix204-2107
α-helix214-2229
α-helix251-2577
α-helix261-2688
α-helix274-2763
α-helix287-2937
α-helix299-31921
α-helix325-3273
α-helix336-3427
α-helix346-3538
α-helix363-3653
β-strand368-37366
β-strand377-38376
α-helix395-4006
α-helix412-4143
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix463-4664
α-helix469-49931
α-helix505-5084
α-helix511-53121
α-helix537-55115
α-helix552-5565
α-helix560-57213
α-helix573-5775
α-helix578-59821
β-strand59917
α-helix630-64112
β-strand65317
α-helix656-66611
α-helix667-6759
α-helix676-68712
α-helix690-71122
β-strand726-73058
β-strand736-73838
β-strand741-74776
Chain C: 28 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix204-2107
α-helix214-2229
α-helix251-2577
α-helix261-2688
α-helix287-2937
α-helix299-31921
α-helix336-3427
α-helix346-3538
α-helix363-3653
β-strand368-37369
β-strand377-38379
α-helix395-4006
α-helix412-4143
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix463-4664
α-helix469-49931
α-helix505-5084
α-helix511-53121
α-helix537-55014
α-helix551-5566
α-helix560-57213
α-helix573-5775
α-helix578-59821
β-strand599110
α-helix630-64112
β-strand653110
α-helix656-66611
α-helix667-6759
α-helix676-68712
α-helix690-71122
β-strand726-730511
β-strand736-738311
β-strand741-74779
Chain D: 30 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix204-2107
α-helix214-2229
α-helix229-2313
α-helix251-2577
α-helix261-2699
α-helix274-2763
α-helix287-2937
α-helix299-31921
α-helix336-3427
α-helix346-3538
α-helix363-3653
β-strand368-37363
β-strand377-38373
α-helix395-4006
α-helix412-4143
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix463-4664
α-helix469-49931
α-helix505-5084
α-helix511-53121
α-helix537-55115
α-helix552-5565
α-helix560-57213
α-helix573-5775
α-helix578-59821
β-strand59914
α-helix630-64112
β-strand65314
α-helix656-66712
α-helix668-6758
α-helix676-68813
α-helix690-71122
β-strand726-73055
β-strand736-73835
β-strand741-74773

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily V member 1A, B, C, Dprotein842Rattus norvegicusO35433 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7L2H_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D)
GAMGSEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSE
EASPLDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRS
IFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALL
LDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFF
KKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVAD
NTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQRE
IHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVE
PLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVT
GEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKE
YVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVV
TLIEDGKNNSLPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFK
AVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCM
RKAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFS
LRSGRVSGRNWKNFALVPLLRDASTRDRHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPG
EK

Ligands and cofactors

IDNameFormulaCopies
XJ7(2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1r,2R,3S,4S,5R,6S)-2,3,4,5,6-pentahydrox…C26 H49 O13 P4
XJD(10R,13S)-16-amino-13-hydroxy-7,13-dioxo-8,12,14-trioxa-13lambda~5~-phosphahexa…C25 H50 N O8 P4

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

Primary citation

Structural snapshots of TRPV1 reveal mechanism of polymodal functionality. Zhang, K., Julius, D., Cheng, Y. Cell (2021) 184:5138. DOI 10.1016/j.cell.2021.08.012 · 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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