eF-site ID 3j5q-ABCDEFGH PDB Code 3j5q Chain A, B, C, D, E, F, G, H click to enlarge Title Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy Classification TRANSPORT PROTEIN/TOXIN Compound Transient receptor potential cation channel subfamily V member 1 Source ORGANISM_SCIENTIFIC: Chilobrachys guangxiensis; Sequence A:  ECRKMFGGCSVDSDCCAHLGCKPTLKYCAWD B:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX C:  ECRKMFGGCSVDSDCCAHLGCKPTLKYCAWD D:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX E:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX F:  ECRKMFGGCSVDSDCCAHLGCKPTLKYCAWD G:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX H:  ECRKMFGGCSVDSDCCAHLGCKPTLKYCAWD Description Functional site 1) 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 2) 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 3) 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 4) 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 5) chain E residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 6) 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 7) chain G residue 144 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 8) chain G residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 9) 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 10) 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 11) 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 12) chain G 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 13) chain A residue 30 type SITE sequence W description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 536-556 type SITE sequence EYVASMVFSLAMGWTNMLYYT description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 572-599 type SITE sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 681-709 type SITE sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain E residue 433-453 type SITE sequence IFYFNFFVYCLYMIIFTAAAY description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain E residue 472-497 type SITE sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain E residue 511-531 type SITE sequence YSEILFFVQSLFMLVSVVLYF description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain E residue 536-556 type SITE sequence EYVASMVFSLAMGWTNMLYYT description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 21) chain E residue 572-599 type SITE sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain E residue 681-709 type SITE sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain G residue 433-453 type SITE sequence IFYFNFFVYCLYMIIFTAAAY description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain C residue 30 type SITE sequence W description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 25) chain G residue 472-497 type SITE sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 26) chain G residue 511-531 type SITE sequence YSEILFFVQSLFMLVSVVLYF description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 27) chain G residue 536-556 type SITE sequence EYVASMVFSLAMGWTNMLYYT description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 28) chain G residue 572-599 type SITE sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 29) chain G residue 681-709 type SITE sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 30) chain F residue 30 type SITE sequence W description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 31) chain H residue 30 type SITE sequence W description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 572-599 type SITE sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 681-709 type SITE sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 433-453 type SITE sequence IFYFNFFVYCLYMIIFTAAAY description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 472-497 type SITE sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 511-531 type SITE sequence YSEILFFVQSLFMLVSVVLYF description Involved in active face => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 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 B residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 39) chain E residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 40) chain G residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 41) chain D residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 42) chain G residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 43) chain G residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 44) chain G residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 45) chain D residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 46) chain D residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 47) chain B residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 48) chain B residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 49) chain B residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 50) chain E residue 115 type BINDING sequence R description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 51) chain E residue 155 type BINDING sequence K description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 52) chain E residue 210 type BINDING sequence E description BINDING => ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI5 53) 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 54) chain G 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 G 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 G 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 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) chain E residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 70) 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 71) chain G residue 498-510 type TOPO_DOM sequence QRRPSVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 72) chain G residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 73) 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 74) chain B 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 75) 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 76) chain G 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 77) chain D residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 78) chain G residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 79) chain G residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 80) chain G residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 81) chain D residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 82) chain D residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 83) chain B residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 84) chain B residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 85) chain B residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 86) chain E residue 160 type BINDING sequence K description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 87) chain E residue 164 type BINDING sequence N description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 88) chain E residue 199 type BINDING sequence Y description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN source Swiss-Prot : SWS_FT_FI6 89) chain D residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 90) chain G residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 91) chain G residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 92) chain G residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 93) chain D residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 94) chain D residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 95) chain B residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 96) chain B residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 97) chain B residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 98) chain E residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 99) chain E residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 100) chain E residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 101) chain D residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 102) chain B residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 103) chain E residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 104) chain G residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 105) 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 106) 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 107) chain E 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 108) chain G 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

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