eF-site ID 5irx-D PDB Code 5irx Chain D click to enlarge Title Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc Classification TRANSPORT PROTEIN Compound Transient receptor potential cation channel subfamily V member 1 Source (DKTX_HAPSC) Sequence D:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT Description (1)  Transient receptor potential cation channel subfamily V member 1, Tau-theraphotoxin-Hs1a Functional site 1) chain D residue 591 type sequence F description binding site for residue 6EU B 803 source : AC7 2) chain D residue 668 type sequence I description binding site for residue 6EU B 803 source : AC7 3) chain D residue 669 type sequence L description binding site for residue 6EU B 803 source : AC7 4) chain D residue 437 type sequence N description binding site for residue 6O8 D 801 source : AD2 5) chain D residue 440 type sequence V description binding site for residue 6O8 D 801 source : AD2 6) chain D residue 487 type sequence Y description binding site for residue 6O8 D 801 source : AD2 7) chain D residue 488 type sequence F description binding site for residue 6O8 D 801 source : AD2 8) chain D residue 491 type sequence R description binding site for residue 6O8 D 801 source : AD2 9) chain D residue 513 type sequence E description binding site for residue 6O8 D 801 source : AD2 10) chain D residue 516 type sequence F description binding site for residue 6O8 D 801 source : AD2 11) chain D residue 554 type sequence Y description binding site for residue 6O8 D 801 source : AD2 12) chain D residue 555 type sequence Y description binding site for residue 6O8 D 801 source : AD2 13) chain D residue 534 type sequence R description binding site for residue 6O9 D 802 source : AD3 14) chain D residue 629 type sequence S description binding site for residue 6OE D 803 source : AD4 15) chain D residue 631 type sequence Y description binding site for residue 6OE D 803 source : AD4 16) chain D residue 532 type sequence S description binding site for residue 6OE D 804 source : AD5 17) chain D residue 534 type sequence R description binding site for residue 6OE D 804 source : AD5 18) chain D residue 511 type sequence Y description binding site for residue 6EU D 805 source : AD6 19) chain D residue 512 type sequence S description binding site for residue 6EU D 805 source : AD6 20) chain D residue 514 type sequence I description binding site for residue 6EU D 805 source : AD6 21) chain D residue 515 type sequence L description binding site for residue 6EU D 805 source : AD6 22) chain D residue 546 type sequence A description binding site for residue 6EU D 805 source : AD6 23) chain D residue 547 type sequence M description binding site for residue 6EU D 805 source : AD6 24) chain D residue 550 type sequence T description binding site for residue 6EU D 805 source : AD6 25) chain D residue 551 type sequence N description binding site for residue 6EU D 805 source : AD6 26) chain D residue 553 type sequence L description binding site for residue 6EU D 805 source : AD6 27) chain D residue 554 type sequence Y description binding site for residue 6EU D 805 source : AD6 28) chain D residue 557 type sequence R description binding site for residue 6EU D 805 source : AD6 29) chain D residue 566 type sequence A description binding site for residue 6EU D 805 source : AD6 30) chain D residue 569 type sequence I description binding site for residue 6EU D 805 source : AD6 31) chain D residue 573 type sequence I description binding site for residue 6EU D 805 source : AD6 32) chain D residue 453 type sequence Y description binding site for residue 6OE E 102 source : AD8 33) chain D 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 34) chain D residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 35) chain D 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 36) chain D residue 727 type MOD_RES sequence Q description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 37) chain D residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 38) chain D residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 39) chain D residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 40) chain D residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 41) chain D residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 42) chain D residue 433-453 type TRANSMEM sequence IFYFNFFVYCLYMIIFTAAAY description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 43) chain D residue 472-497 type TRANSMEM sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 44) chain D residue 511-531 type TRANSMEM sequence YSEILFFVQSLFMLVSVVLYF description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 45) chain D residue 536-556 type TRANSMEM sequence EYVASMVFSLAMGWTNMLYYT description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 46) chain D residue 572-599 type TRANSMEM sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 47) chain D residue 681-709 type TRANSMEM sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 48) chain D residue 498-510 type TOPO_DOM sequence QRRPSLKSLFVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 49) chain D residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 50) chain D residue 454-471 type TOPO_DOM sequence YRPVEGLPPYKLKNTVGD description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 532-535 type TOPO_DOM sequence SQRK description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 52) chain D residue 600-649 type TOPO_DOM sequence EDGKYNSLYSTCLELFKFTIGMGDLEF description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2

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