eF-site ID 3j5q-E PDB Code 3j5q Chain E 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 E:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX Description Functional site 1) chain E residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 2) chain E residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 3) chain E 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 4) chain E residue 433-453 type SITE sequence IFYFNFFVYCLYMIIFTAAAY description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain E residue 472-497 type SITE sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain E residue 511-531 type SITE sequence YSEILFFVQSLFMLVSVVLYF description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 7) chain E residue 536-556 type SITE sequence EYVASMVFSLAMGWTNMLYYT description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 8) chain E residue 572-599 type SITE sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 9) chain E residue 681-709 type SITE sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain E residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 11) chain E residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 12) chain E residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 13) chain E residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 14) chain E residue 454-471 type TOPO_DOM sequence YRPVEGLPPYKLKNTVGD description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 15) chain E residue 532-535 type TOPO_DOM sequence SQRK description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 16) chain E residue 600-649 type TOPO_DOM sequence EDGKYNSLYSTCLELFKFTIGMGDLEF description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 17) chain E residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 18) chain E residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 19) chain E 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 20) chain E residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 21) chain E residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 22) chain E residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 23) chain E residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 24) chain E residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 25) chain E residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 26) chain E residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 27) chain E 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

Display surface Download Links