eF-site ID 5is0-C PDB Code 5is0 Chain C click to enlarge Title Structure of TRPV1 in complex with capsazepine, determined in lipid nanodisc Classification TRANSPORT PROTEIN Compound Transient receptor potential cation channel subfamily V member 1 Source (TRPV1_RAT) Sequence C:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT Description Functional site 1) chain C residue 511 type sequence Y description binding site for residue 6ET C 801 source : AC1 2) chain C residue 512 type sequence S description binding site for residue 6ET C 801 source : AC1 3) chain C residue 515 type sequence L description binding site for residue 6ET C 801 source : AC1 4) chain C residue 543 type sequence F description binding site for residue 6ET C 801 source : AC1 5) chain C residue 550 type sequence T description binding site for residue 6ET C 801 source : AC1 6) chain C residue 551 type sequence N description binding site for residue 6ET C 801 source : AC1 7) chain C residue 553 type sequence L description binding site for residue 6ET C 801 source : AC1 8) chain C residue 570 type sequence E description binding site for residue 6ET C 801 source : AC1 9) chain C residue 669 type sequence L description binding site for residue 6ET D 801 source : AC3 10) 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 11) 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 12) 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 13) 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 14) 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 15) 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 16) 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 17) 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 18) chain C residue 704 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 19) chain C residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 20) 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 21) 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 22) 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 23) 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 24) 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 25) 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 26) chain C residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 27) chain C residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 28) chain C residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 29) chain C residue 646 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8

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