3J5P: PDB entry 3J5P

Structure of TRPV1 ion channel determined by single particle electron cryo-microscopy. Determined by electron microscopy at 3.27 Å resolution. Released 4 Dec 2013.

Method: Electron microscopy
Resolution: 3.27 Å
Organism: Rattus norvegicus
Chains: 4
Atoms: 18,636
Mol. weight: 272.97 kDa
Released: 4 Dec 2013

Explore 3J5P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3J5P contains 140 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.

Chains A, B, C and D: 35 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	114-122	9
α-helix	132-138	7
α-helix	146-148	3
α-helix	157-163	7
β-strand	166	1	4
β-strand	169	1	4
α-helix	171-182	12
α-helix	186-190	5
α-helix	204-210	7
α-helix	214-222	9
β-strand	231	1	5
α-helix	234-236	3
β-strand	249	1	5
α-helix	251-257	7
α-helix	261-269	9
α-helix	287-294	8
α-helix	299-319	21
α-helix	328-330	3
α-helix	336-342	7
α-helix	346-353	8
α-helix	362-365	4
β-strand	368-369	2	6
β-strand	378-382	5	6
α-helix	385-388	4
α-helix	395-400	6
α-helix	412-414	3
α-helix	416-425	10
α-helix	426-430	5
α-helix	431-454	24
α-helix	462-466	5
α-helix	469-497	29
α-helix	511-532	22
α-helix	537-551	15
α-helix	552-556	5
α-helix	560-571	12
α-helix	572-577	6
α-helix	578-598	21
α-helix	630-642	13
α-helix	656-665	10
α-helix	666-672	7
α-helix	673-710	38
β-strand	753-757	5	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transient receptor potential cation channel subfamily V member 1	A, B, C, D	protein	598	Rattus norvegicus	O35433 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3J5P_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D)
LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQN
DTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA
ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHA
LVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA
YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRH
DMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG
DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLY
FSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFG
FSTAVVTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYIL
LLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAXXXXXXXXXXXX

Primary citation

Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Liao, M., Cao, E., Julius, D. et al. Nature (2013) 504:107-112. DOI 10.1038/nature12822 · PubMed

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

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3J5P is part of these collections:

Ion channels

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