7L2S: DkTx-bound minimal TRPV1 at the pre-bound state

cryo-EM structure of DkTx-bound minimal TRPV1 at the pre-bound state. Determined by electron microscopy at 2.71 Å resolution. Released 22 Sept 2021.

Method
Electron microscopy
Resolution
2.71 Å
Organism
Rattus norvegicus
Chains
4
Atoms
20,579
Mol. weight
296.75 kDa
Ligands
6IY, XJ7
Released
22 Sept 2021

Explore 7L2S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7L2S contains 150 α-helices and 38 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: 39 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix115-1239
α-helix126-1294
α-helix132-1398
α-helix146-1483
α-helix157-1637
β-strand16616
β-strand16916
α-helix172-18312
α-helix187-1904
β-strand19317
β-strand20317
α-helix204-2107
α-helix214-2229
α-helix234-2363
α-helix251-2577
α-helix261-2699
α-helix287-2937
α-helix299-31921
α-helix325-3273
α-helix336-3438
α-helix346-3538
α-helix363-3653
β-strand368-37368
β-strand377-38268
α-helix395-4006
α-helix412-4143
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix463-4664
α-helix469-49931
α-helix503-5086
α-helix511-53121
α-helix537-55014
α-helix551-5566
α-helix560-57213
α-helix573-5775
α-helix578-59821
α-helix630-6389
α-helix639-6424
α-helix656-66712
α-helix668-6747
α-helix675-68612
α-helix690-71122
β-strand72619
β-strand73819
β-strand742-74768
α-helix753-7553
Chain B: 36 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix115-1239
α-helix127-1315
α-helix132-1398
α-helix146-1483
α-helix157-1637
β-strand166110
β-strand169110
α-helix172-18312
α-helix187-1904
β-strand193111
β-strand203111
α-helix204-2107
α-helix214-2229
α-helix251-2577
α-helix261-2699
α-helix287-2937
α-helix299-31921
α-helix325-3273
α-helix336-3438
α-helix346-3538
α-helix363-3653
β-strand368-373612
β-strand377-382612
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-helix630-6389
α-helix656-66611
α-helix667-6748
α-helix675-68612
α-helix690-71122
β-strand726113
β-strand738113
β-strand742-747612
Chain C: 38 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix114-12310
α-helix126-1316
α-helix135-1395
α-helix146-1483
α-helix157-1626
β-strand166114
β-strand169114
α-helix172-18312
α-helix187-1904
β-strand193115
β-strand203115
α-helix204-2107
α-helix214-2229
α-helix234-2363
α-helix251-2577
α-helix261-2699
α-helix287-2948
α-helix299-31921
α-helix325-3273
α-helix336-3438
α-helix346-3538
α-helix363-3653
β-strand368-373616
β-strand377-382616
α-helix395-4006
α-helix412-4143
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix462-4654
α-helix469-49931
α-helix505-5084
α-helix511-53020
α-helix537-55014
α-helix551-5566
α-helix560-57213
α-helix573-5775
α-helix578-59821
α-helix630-6389
α-helix639-6424
α-helix656-66611
α-helix667-6748
α-helix675-68612
α-helix690-71122
β-strand726117
β-strand738117
β-strand742-747616
Chain D: 37 helices, 11 β-strands
ElementResiduesLengthSheet
α-helix115-1239
α-helix127-1293
α-helix132-1398
α-helix146-1483
β-strand14911
β-strand15611
α-helix157-1637
β-strand16612
β-strand16912
α-helix172-18312
α-helix187-1904
β-strand19313
β-strand20313
α-helix204-2107
α-helix214-2229
α-helix234-2363
α-helix251-2577
α-helix261-2699
α-helix287-2937
α-helix299-31921
α-helix325-3273
α-helix336-3438
α-helix346-3538
α-helix363-3653
β-strand368-37364
β-strand377-38264
α-helix395-4006
α-helix412-4143
α-helix416-42510
α-helix426-4305
α-helix431-45323
α-helix463-4642
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-helix630-6389
α-helix656-66712
α-helix668-6747
α-helix675-68612
α-helix690-71122
β-strand72615
β-strand73815
β-strand742-74764

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily V member 1A, B, C, Dprotein637Rattus norvegicusO35433 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7L2S_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D)
GAMGSRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLN
LHNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENG
ADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVG
NTVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSG
KIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSS
ETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYK
LKNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFML
VSVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVY
LVFLFGFSTAVVTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYV
ILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQ
VGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPG

Ligands and cofactors

IDNameFormulaCopies
6IY(10R,13S)-16-amino-13-hydroxy-7,13-dioxo-8,12,14-trioxa-13lambda~5~-phosphahexa…C28 H56 N O8 P4
XJ7(2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1r,2R,3S,4S,5R,6S)-2,3,4,5,6-pentahydrox…C26 H49 O13 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) 184:5138-5150.e12. 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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