9W4T: RatTRPV1

ratTRPV1 bound with antagonist AMG9810. Determined by electron microscopy at 2.87 Å resolution. Released 26 Nov 2025.

Method

Electron microscopy

Resolution

2.87 Å

Organisms

Escherichia coli K-12, Rattus norvegicus

Chains

4

Atoms

17,525

Mol. weight

563.24 kDa

Ligands

A1D6W

Released

26 Nov 2025

Explore 9W4T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9W4T contains 105 α-helices and 28 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: 26 helices, 7 β-strands

Molecules and chains

>9W4T_1 Maltose/maltodextrin-binding periplasmic protein,Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE
ALKDAQTNSGTGGGSGDDDDKSPMGSHHHHHHHHGSDYDIPTTENLYFQGAMDPMEQRAS
LDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASPLDCPYE
EGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRSIFDAVAQSNC
QELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSL
KQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFFKKTKGRPGFY
FGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTVDNTKFVT
SMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEPECRHLS
RKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKW
DRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEILSVSGGV
YFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVASMVFSLA
MGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNS
LPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAY
VILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLL
QVGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRN
WKNFALVPLLRDASTRDRHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPGEK

Ligands and cofactors

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

Primary citation

Structures of TRPV1 bound by hyperthermia-inducing analgesics. Gao, Y.H., Huang, Y.Z., Li, Z.X. et al. Cell Rep (2026) 45:116765-116765. DOI 10.1016/j.celrep.2025.116765 · PubMed

Related structures

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

• 3SUI 1.95 Å, Crystal structure of ca2+-calmodulin in complex with a trpv1 c-terminal peptide
• 8U4D 2.2 Å, TRPV1 in nanodisc bound with PI-Br4, consensus structure
• 8U3A 2.3 Å, TRPV1 in nanodisc bound with PI-Br4 bound in Conformation 1 (monomer)
• 8U3C 2.3 Å, TRPV1 in nanodisc bound with PI-Br4 bound in Conformation 2 (monomer)
• 8U43 2.4 Å, TRPV1 in nanodisc bound with PIP2-Br4
• 7L2P 2.6 Å, cryo-EM structure of unliganded minimal TRPV1
• 7L2H 2.63 Å, Cryo-EM structure of unliganded full-length TRPV1 at neutral pH
• 7LP9 2.63 Å, Cryo-EM structure of full-length TRPV1 at 4 degrees Celsius
• 2PNN 2.7 Å, Crystal Structure of the Ankyrin Repeat Domain of Trpv1
• 9W4M 2.7 Å, ratTRPV1 bound with antagonist AMG517
• 7L2S 2.71 Å, cryo-EM structure of DkTx-bound minimal TRPV1 at the pre-bound state
• 7MZ5 2.76 Å, Cryo-EM structure of RTX-bound full-length TRPV1 in C2 state

Browse structure collections

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