eF-site ID 5is0-BCDE PDB Code 5is0 Chain B, C, D, E 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 B:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT C:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT D:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT E:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT Description Functional site 1) chain B residue 669 type sequence L description binding site for residue 6ET C 801 source : AC1 2) chain C residue 511 type sequence Y description binding site for residue 6ET C 801 source : AC1 3) chain C residue 512 type sequence S description binding site for residue 6ET C 801 source : AC1 4) chain C residue 515 type sequence L description binding site for residue 6ET C 801 source : AC1 5) chain C residue 543 type sequence F description binding site for residue 6ET C 801 source : AC1 6) chain C residue 550 type sequence T description binding site for residue 6ET C 801 source : AC1 7) chain C residue 551 type sequence N description binding site for residue 6ET C 801 source : AC1 8) chain C residue 553 type sequence L description binding site for residue 6ET C 801 source : AC1 9) chain C residue 570 type sequence E description binding site for residue 6ET C 801 source : AC1 10) chain B residue 511 type sequence Y description binding site for residue 6ET B 801 source : AC2 11) chain B residue 512 type sequence S description binding site for residue 6ET B 801 source : AC2 12) chain B residue 515 type sequence L description binding site for residue 6ET B 801 source : AC2 13) chain B residue 543 type sequence F description binding site for residue 6ET B 801 source : AC2 14) chain B residue 550 type sequence T description binding site for residue 6ET B 801 source : AC2 15) chain B residue 551 type sequence N description binding site for residue 6ET B 801 source : AC2 16) chain B residue 553 type sequence L description binding site for residue 6ET B 801 source : AC2 17) chain B residue 570 type sequence E description binding site for residue 6ET B 801 source : AC2 18) chain E residue 669 type sequence L description binding site for residue 6ET B 801 source : AC2 19) chain C residue 669 type sequence L description binding site for residue 6ET D 801 source : AC3 20) chain D residue 511 type sequence Y description binding site for residue 6ET D 801 source : AC3 21) chain D residue 512 type sequence S description binding site for residue 6ET D 801 source : AC3 22) chain D residue 515 type sequence L description binding site for residue 6ET D 801 source : AC3 23) chain D residue 543 type sequence F description binding site for residue 6ET D 801 source : AC3 24) chain D residue 550 type sequence T description binding site for residue 6ET D 801 source : AC3 25) chain D residue 551 type sequence N description binding site for residue 6ET D 801 source : AC3 26) chain D residue 553 type sequence L description binding site for residue 6ET D 801 source : AC3 27) chain D residue 570 type sequence E description binding site for residue 6ET D 801 source : AC3 28) chain D residue 669 type sequence L description binding site for residue 6ET E 801 source : AC4 29) chain E residue 511 type sequence Y description binding site for residue 6ET E 801 source : AC4 30) chain E residue 512 type sequence S description binding site for residue 6ET E 801 source : AC4 31) chain E residue 515 type sequence L description binding site for residue 6ET E 801 source : AC4 32) chain E residue 543 type sequence F description binding site for residue 6ET E 801 source : AC4 33) chain E residue 550 type sequence T description binding site for residue 6ET E 801 source : AC4 34) chain E residue 551 type sequence N description binding site for residue 6ET E 801 source : AC4 35) chain E residue 553 type sequence L description binding site for residue 6ET E 801 source : AC4 36) chain E residue 570 type sequence E description binding site for residue 6ET E 801 source : AC4 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) chain D residue 658-686 type TRANSMEM sequence VFIILLLAYVILTYILLLNMLIALMGETV description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 54) 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 55) 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 56) 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 57) 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 58) 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 59) chain B residue 681-709 type TRANSMEM sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) chain B residue 498-510 type TOPO_DOM sequence QRRPSLKSLFVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 76) 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 77) chain D residue 498-510 type TOPO_DOM sequence QRRPSLKSLFVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 78) 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 79) 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 80) 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 81) 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 82) chain D 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 83) 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 84) 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 85) chain E residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 86) chain E residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 87) chain E residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 88) chain B residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 89) chain B residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 90) chain D residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 91) chain D residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 92) chain D residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 93) chain C residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 94) chain C residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 95) chain C residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 96) chain B residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 97) chain C residue 646 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 98) chain D residue 646 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 99) chain B residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 100) chain E residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 101) 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 102) 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 103) 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 104) 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 105) 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 106) 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 107) 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 108) 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 109) chain C residue 704 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 110) chain D residue 704 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 111) chain B residue 727 type MOD_RES sequence Q description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 112) chain E residue 727 type MOD_RES sequence Q description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 113) chain C residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 114) chain B residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 115) chain D residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 116) chain E residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13

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