eF-site ID 5irx-C PDB Code 5irx Chain C 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 C:  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 C residue 453 type sequence Y description binding site for residue 6OE A 802 source : AC2 2) chain C residue 437 type sequence N description binding site for residue 6O8 C 801 source : AC8 3) chain C residue 440 type sequence V description binding site for residue 6O8 C 801 source : AC8 4) chain C residue 487 type sequence Y description binding site for residue 6O8 C 801 source : AC8 5) chain C residue 488 type sequence F description binding site for residue 6O8 C 801 source : AC8 6) chain C residue 491 type sequence R description binding site for residue 6O8 C 801 source : AC8 7) chain C residue 513 type sequence E description binding site for residue 6O8 C 801 source : AC8 8) chain C residue 516 type sequence F description binding site for residue 6O8 C 801 source : AC8 9) chain C residue 554 type sequence Y description binding site for residue 6O8 C 801 source : AC8 10) chain C residue 555 type sequence Y description binding site for residue 6O8 C 801 source : AC8 11) chain C residue 534 type sequence R description binding site for residue 6OE C 802 source : AC9 12) chain C residue 511 type sequence Y description binding site for residue 6EU C 803 source : AD1 13) chain C residue 512 type sequence S description binding site for residue 6EU C 803 source : AD1 14) chain C residue 514 type sequence I description binding site for residue 6EU C 803 source : AD1 15) chain C residue 515 type sequence L description binding site for residue 6EU C 803 source : AD1 16) chain C residue 546 type sequence A description binding site for residue 6EU C 803 source : AD1 17) chain C residue 547 type sequence M description binding site for residue 6EU C 803 source : AD1 18) chain C residue 550 type sequence T description binding site for residue 6EU C 803 source : AD1 19) chain C residue 551 type sequence N description binding site for residue 6EU C 803 source : AD1 20) chain C residue 553 type sequence L description binding site for residue 6EU C 803 source : AD1 21) chain C residue 554 type sequence Y description binding site for residue 6EU C 803 source : AD1 22) chain C residue 557 type sequence R description binding site for residue 6EU C 803 source : AD1 23) chain C residue 566 type sequence A description binding site for residue 6EU C 803 source : AD1 24) chain C residue 569 type sequence I description binding site for residue 6EU C 803 source : AD1 25) chain C residue 573 type sequence I description binding site for residue 6EU C 803 source : AD1 26) chain C residue 591 type sequence F description binding site for residue 6EU D 805 source : AD6 27) chain C residue 668 type sequence I description binding site for residue 6EU D 805 source : AD6 28) chain C residue 669 type sequence L description binding site for residue 6EU D 805 source : AD6 29) chain C residue 534 type sequence R description binding site for residue 6O9 E 101 source : AD7 30) chain C residue 629 type sequence S description binding site for residue 6OE E 102 source : AD8 31) chain C residue 631 type sequence Y description binding site for residue 6OE E 102 source : AD8 32) chain C residue 627-649 type INTRAMEM sequence YNSLYSTCLELFKFTIGMGDLEF description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 source Swiss-Prot : SWS_FT_FI4 33) 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 34) 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 35) chain C residue 704 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 36) chain C residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 37) chain C residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 38) chain C residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 39) chain C residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 40) chain C residue 646 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 41) 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 42) 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 43) 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 44) 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 45) 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 46) chain C residue 658-686 type TRANSMEM sequence VFIILLLAYVILTYILLLNMLIALMGETV description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 47) chain C residue 498-510 type TOPO_DOM sequence QRRPSLKSLFVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 48) 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 49) 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 50) 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 51) 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

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