eF-site ID 3j5p-ABCD PDB Code 3j5p Chain A, B, C, D click to enlarge Title Structure of TRPV1 ion channel determined by single particle electron cryo-microscopy Classification TRANSPORT PROTEIN Compound Transient receptor potential cation channel subfamily V member 1 Source (3J5P) Sequence A:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX B:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX C:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX D:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX Description Functional site 1) chain B residue 433-453 type TRANSMEM sequence IFYFNFFVYCLYMIIFTAAAY description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 536-556 type TRANSMEM sequence EYVASMVFSLAMGWTNMLYYT description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 572-599 type TRANSMEM sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 659-687 type TRANSMEM sequence FIILLLAYVILTYILLLNMLIALMGETVN description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 5) 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 6) 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 7) 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 8) 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 9) 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 10) chain C residue 659-687 type TRANSMEM sequence FIILLLAYVILTYILLLNMLIALMGETVN description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 11) 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 12) chain B residue 472-497 type TRANSMEM sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 13) 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 14) 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 15) 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 16) 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 17) chain D residue 659-687 type TRANSMEM sequence FIILLLAYVILTYILLLNMLIALMGETVN description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 511-531 type TRANSMEM sequence YSEILFFVQSLFMLVSVVLYF description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 536-556 type TRANSMEM sequence EYVASMVFSLAMGWTNMLYYT description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 572-599 type TRANSMEM sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 659-687 type TRANSMEM sequence FIILLLAYVILTYILLLNMLIALMGETVN description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 433-453 type TRANSMEM sequence IFYFNFFVYCLYMIIFTAAAY description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 472-497 type TRANSMEM sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 511-531 type TRANSMEM sequence YSEILFFVQSLFMLVSVVLYF description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 26) chain B residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 27) chain A residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 28) chain A residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 29) chain C residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 30) 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 31) chain D residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 32) 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 33) chain B 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 34) chain A 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 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 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 37) chain B residue 705 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 38) chain A residue 705 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 39) chain C residue 705 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 40) chain D residue 705 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 41) chain B residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 42) chain A residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 43) chain C residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 44) chain D residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 45) chain B residue 454-471 type TOPO_DOM sequence YRPVEGLPPYKLKNTVGD description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 46) 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 47) 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 48) 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 49) chain B residue 532-535 type TOPO_DOM sequence SQRK description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 600-649 type TOPO_DOM sequence EDGKYNSLYSTCLELFKFTIGMGDLEF description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 454-471 type TOPO_DOM sequence YRPVEGLPPYKLKNTVGD description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 532-535 type TOPO_DOM sequence SQRK description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 600-649 type TOPO_DOM sequence EDGKYNSLYSTCLELFKFTIGMGDLEF description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 54) 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 55) 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 56) 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 57) chain B residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 58) chain B residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 60) chain A residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 61) chain C residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 62) 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 63) chain D residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 64) 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 65) chain B residue 628-650 type INTRAMEM sequence NSLYSTCLELFKFTIGMGDLEFT description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 source Swiss-Prot : SWS_FT_FI4 66) chain A residue 628-650 type INTRAMEM sequence NSLYSTCLELFKFTIGMGDLEFT description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 source Swiss-Prot : SWS_FT_FI4 67) chain C residue 628-650 type INTRAMEM sequence NSLYSTCLELFKFTIGMGDLEFT description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 source Swiss-Prot : SWS_FT_FI4 68) chain D residue 628-650 type INTRAMEM sequence NSLYSTCLELFKFTIGMGDLEFT description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 source Swiss-Prot : SWS_FT_FI4 69) chain B residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 70) chain D residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 71) chain D residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 72) chain D residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 73) chain B residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 74) chain B residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 75) chain A residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 76) chain A residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 77) chain A residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 78) chain C residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 79) chain C residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 80) chain C residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 81) chain B residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 82) chain D residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 83) chain D residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 84) chain D residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 85) chain B residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 86) chain B residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 87) chain A residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 88) chain A residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 89) chain A residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 90) chain C residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 91) chain C residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 92) chain C residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 93) chain B residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 94) chain D residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 95) chain D residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 96) chain D residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 97) chain B residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 98) chain B residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 99) chain A residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 100) chain A residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 101) chain A residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 102) chain C residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 103) chain C residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 104) chain C residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 105) chain B residue 647 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 106) chain A residue 647 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 107) chain C residue 647 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 108) chain D residue 647 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 109) chain B 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 110) chain A 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 111) chain C 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 112) chain D 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