eF-site ID 5irz-E PDB Code 5irz Chain E click to enlarge Title Structure of TRPV1 determined in lipid nanodisc Classification TRANSPORT PROTEIN Compound Transient receptor potential cation channel subfamily V member 1 Source (TRPV1_RAT) Sequence E:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT Description Functional site 1) chain E residue 657 type sequence A description binding site for residue 6OE D 803 source : AC3 2) chain E residue 589 type sequence F description binding site for residue 6OE D 805 source : AC5 3) chain E residue 629 type sequence S description binding site for residue 6OE D 805 source : AC5 4) chain E residue 437 type sequence N description binding site for residue 6O8 E 801 source : AC7 5) chain E residue 440 type sequence V description binding site for residue 6O8 E 801 source : AC7 6) chain E residue 488 type sequence F description binding site for residue 6O8 E 801 source : AC7 7) chain E residue 491 type sequence R description binding site for residue 6O8 E 801 source : AC7 8) chain E residue 513 type sequence E description binding site for residue 6O8 E 801 source : AC7 9) chain E residue 516 type sequence F description binding site for residue 6O8 E 801 source : AC7 10) chain E residue 554 type sequence Y description binding site for residue 6O8 E 801 source : AC7 11) chain E residue 555 type sequence Y description binding site for residue 6O8 E 801 source : AC7 12) chain E residue 509 type sequence D description binding site for residue 6ES E 802 source : AC8 13) chain E residue 510 type sequence S description binding site for residue 6ES E 802 source : AC8 14) chain E residue 511 type sequence Y description binding site for residue 6ES E 802 source : AC8 15) chain E residue 512 type sequence S description binding site for residue 6ES E 802 source : AC8 16) chain E residue 550 type sequence T description binding site for residue 6ES E 802 source : AC8 17) chain E residue 557 type sequence R description binding site for residue 6ES E 802 source : AC8 18) chain E residue 570 type sequence E description binding site for residue 6ES E 802 source : AC8 19) chain E residue 699 type sequence L description binding site for residue 6ES E 802 source : AC8 20) chain E residue 700 type sequence Q description binding site for residue 6ES E 802 source : AC8 21) chain E residue 655 type sequence F description binding site for residue 6OE E 803 source : AC9 22) chain E residue 453 type sequence Y description binding site for residue 6OE E 804 source : AD1 23) chain E residue 454 type sequence Y description binding site for residue 6OE E 804 source : AD1 24) chain E residue 454 type sequence Y description binding site for residue 6OE E 805 source : AD2 25) chain E residue 470 type sequence G description binding site for residue 6OE E 805 source : AD2 26) chain E residue 473 type sequence F description binding site for residue 6OE E 805 source : AD2 27) chain E residue 474 type sequence R description binding site for residue 6OE E 805 source : AD2 28) chain E residue 631 type sequence Y description binding site for residue 6OE E 806 source : AD3 29) 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 30) 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 31) chain E residue 536-556 type TRANSMEM sequence EYVASMVFSLAMGWTNMLYYT description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 32) chain E residue 572-599 type TRANSMEM sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 33) chain E residue 681-709 type TRANSMEM sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 34) chain E residue 433-453 type TRANSMEM sequence IFYFNFFVYCLYMIIFTAAAY description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 35) chain E residue 472-497 type TRANSMEM sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 36) chain E residue 511-531 type TRANSMEM sequence YSEILFFVQSLFMLVSVVLYF description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 37) chain E residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 38) 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 39) 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 40) 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 41) chain E residue 498-510 type TOPO_DOM sequence QRRPSLKSLFVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 42) 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 43) 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 44) chain E residue 727 type MOD_RES sequence Q description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 45) chain E residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 46) chain E residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 47) chain E residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 48) chain E residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8

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