eF-site ID 3j5q-B PDB Code 3j5q Chain B click to enlarge Title Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy Classification TRANSPORT PROTEIN/TOXIN Compound Transient receptor potential cation channel subfamily V member 1 Source ORGANISM_SCIENTIFIC: Chilobrachys guangxiensis; Sequence B:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX Description Functional site 1) chain B 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 2) chain B residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 3) chain B residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 4) chain B residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 5) chain B residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 6) chain B residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 7) chain B residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 8) chain B residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 9) chain B residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 10) chain B residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 11) chain B residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 12) chain B residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 13) chain B 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 B residue 433-453 type SITE sequence IFYFNFFVYCLYMIIFTAAAY description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 472-497 type SITE sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 511-531 type SITE sequence YSEILFFVQSLFMLVSVVLYF description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 536-556 type SITE sequence EYVASMVFSLAMGWTNMLYYT description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 572-599 type SITE sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 681-709 type SITE sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 454-471 type TOPO_DOM sequence YRPVEGLPPYKLKNTVGD description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 532-535 type TOPO_DOM sequence SQRK description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 600-649 type TOPO_DOM sequence EDGKYNSLYSTCLELFKFTIGMGDLEF description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 25) chain B 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 26) chain B residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 27) chain B residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10

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