eF-site ID 3j5p-C PDB Code 3j5p Chain C click to enlarge Title Structure of TRPV1 ion channel determined by single particle electron cryo-microscopy Classification TRANSPORT PROTEIN Compound Transient receptor potential cation channel subfamily V member 1 Source (3J5P) Sequence C:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX Description Functional site 1) chain C residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 2) chain C residue 650-672 type INTRAMEM sequence TENYDFKAVFIILLLAYVILTYI description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 source Swiss-Prot : SWS_FT_FI4 3) chain C residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 4) chain C residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 5) chain C residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 6) chain C residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 7) chain C residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 8) chain C residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 9) chain C residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 10) chain C residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 11) chain C residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 12) chain C residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 13) chain C residue 116 type MOD_RES sequence S description Phosphoserine; by PKA and PKD => ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:15471852 source Swiss-Prot : SWS_FT_FI9 14) chain C residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 15) chain C residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 16) chain C residue 502 type MOD_RES sequence S description Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI11 17) chain C residue 758 type MOD_RES sequence X description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 18) chain C residue 433-453 type TRANSMEM sequence IFYFNFFVYCLYMIIFTAAAY description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 472-497 type TRANSMEM sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 511-531 type TRANSMEM sequence YSEILFFVQSLFMLVSVVLYF description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 536-556 type TRANSMEM sequence EYVASMVFSLAMGWTNMLYYT description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 572-599 type TRANSMEM sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 23) chain C residue 681-709 type TRANSMEM sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 24) chain C residue 454-471 type TOPO_DOM sequence YRPVEGLPPYKLKNTVGD description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 532-535 type TOPO_DOM sequence SQRK description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 26) chain C residue 600-649 type TOPO_DOM sequence EDGKYNSLYSTCLELFKFTIGMGDLEF description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3

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