eF-site ID 4u5c-ABCDEF PDB Code 4u5c Chain A, B, C, D, E, F click to enlarge Title Crystal structure of GluA2, con-ikot-ikot snail toxin, partial agonist FW and postitive modulator (R,R)-2b complex Classification Transport protein/toxin Compound Glutamate receptor 2 Source (CONII_CONST) Sequence A:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNID ETYRSLFQDLELKGERRVILDCERDKVNDIVDQVITIGKH VKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDYDDSL VSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTE AFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALK QVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYW SEVDKMVVTLTESGDGLEQKTVVVTTILESPYVMMKKNHE MLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGAR DADTKIWDGMVGELVYGKADIAIAPLTITLVREEVIDFSK PFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMAIVFAY ILVSVVLFLVSSPRSLSARIVAGVWWFFTLIIISSYTANL AAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFR RSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKY AYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS SLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGSALSLS NVAGVFYILVGGLGLAMLVALIEFAYK B:  SIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNL EVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCG TLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQW DKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINN DKKDETYRSLFQDLELKGERRVILDCERDKVNDIVDQVIT IGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDY DDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQ VMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIE RALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRK IGYWSEVDKMVVTLTESGGLEQKTVVVTTILESPYVMMKK NHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKY GARDADTKIWDGMVGELVYGKADIAIAPLTITLVREEVID FSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMAIV FAYILVSVVLFLSPRSLSARIVAGVWWFFTLIIISSYTAN LAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFF RRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGK YAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKG SSLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGSLSNV AGVFYILVGGLGLAMLVALIEFAYKR C:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKGERRVILDCERDKVNDIVDQVI TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR KIGYWSEVDKMVVTLTTSGLEQKTVVVTTILESPYVMMKK NHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKY GARDADTKIWDGMVGELVYGKADIAIAPLTITLVREEVID FSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMAIV FAYILVSVVLFLVSPRSLSARIVAGVWWFFTLIIISSYTA NLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEF FRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKG KYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPK GSSLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGSLSN VAGVFYILVGGLGLAMLVALIEFAY D:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKGERRVILDCERDKVNDIVDQVI TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR KIGYWSEVDKMVVTLTSGLEQKTVVVTTILESPYVMMKKN HEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYG ARDADTKIWDGMVGELVYGKADIAIAPLTITLVREEVIDF SKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMAIVF AYILVSVVLFLVSRADISPRSLSARIVAGVWWFFTLIIIS SYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGS TKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVR KSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGI ATPKGSSLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECG AKDSALSLSNVAGVFYILVGGLGLAMLVALIEF E:  GPADCCRMKECCTDRVNECLQRYSGREDKFVSFCYQEATV TCGSFNEIVGCCYGYQMCMIRVVKPNSLSGAHEACKTVSC GNPCA F:  GPADCCRMKECCTDRVNECLQRYSGREDKFVSFCYQEATV TCGSFNEIVGCCYGYQMCMIRVVKPNSLSGAHEACKTVSC GNPCA Description Functional site 1) chain A residue 596 type LIPID sequence L description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 2) chain B residue 596 type LIPID sequence L description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 3) chain C residue 596 type LIPID sequence L description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 4) chain D residue 596 type LIPID sequence L description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 5) chain A residue 237 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 6) chain B residue 237 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 7) chain C residue 237 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 8) chain D residue 237 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 9) chain A residue 351 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI16 10) chain B residue 351 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI16 11) chain C residue 351 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI16 12) chain D residue 351 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI16 13) chain A residue 394 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 14) chain B residue 394 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 15) chain C residue 387 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 16) chain C residue 394 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 17) chain D residue 394 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 18) chain E residue 37 type SITE sequence Q description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 19) chain E residue 48 type SITE sequence E description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 20) chain E residue 75 type SITE sequence A description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 21) chain F residue 37 type SITE sequence Q description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 22) chain F residue 48 type SITE sequence E description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 23) chain F residue 75 type SITE sequence A description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 24) chain D residue 525-545 type SITE sequence IWMAIVFAYILVSVVLFLVSR description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 603-623 type SITE sequence GVWWFFTLIIISSYTANLAAF description Interaction with glutamate receptor 2 (GRIA2) => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 597-602 type TOPO_DOM sequence SARIVA description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 27) chain D residue 597-602 type TOPO_DOM sequence SARIVA description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 28) chain A residue 597-602 type TOPO_DOM sequence SARIVA description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 29) chain B residue 597-602 type TOPO_DOM sequence SARIVA description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 30) chain A residue 594-596 type INTRAMEM sequence RSL description source Swiss-Prot : SWS_FT_FI4 31) chain B residue 594-596 type INTRAMEM sequence RSL description source Swiss-Prot : SWS_FT_FI4 32) chain C residue 594-596 type INTRAMEM sequence RSL description source Swiss-Prot : SWS_FT_FI4 33) chain D residue 594-596 type INTRAMEM sequence RSL description source Swiss-Prot : SWS_FT_FI4 34) chain A residue 624-798 type TOPO_DOM sequence LTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSK IAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYL LESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLG TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGSALSLSNVA GVFYI description Extracellular source Swiss-Prot : SWS_FT_FI5 35) chain B residue 624-798 type TOPO_DOM sequence LTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSK IAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYL LESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLG TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGSLSNVAGVF YI description Extracellular source Swiss-Prot : SWS_FT_FI5 36) chain C residue 624-798 type TOPO_DOM sequence LTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSK IAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYL LESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLG TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGSLSNVAGVF YI description Extracellular source Swiss-Prot : SWS_FT_FI5 37) chain D residue 624-798 type TOPO_DOM sequence LTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSK IAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYL LESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLG TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSALSLS NVAGVFYI description Extracellular source Swiss-Prot : SWS_FT_FI5 38) chain A residue 452 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 39) chain D residue 452 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 40) chain D residue 487 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 41) chain D residue 712 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 42) chain B residue 487 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 43) chain B residue 712 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 44) chain C residue 452 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 45) chain C residue 487 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 46) chain C residue 712 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 47) chain A residue 487 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 48) chain A residue 712 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 49) chain B residue 452 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 50) chain A residue 480 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 51) chain B residue 480 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 52) chain C residue 480 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 53) chain D residue 480 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 54) chain C residue 482 type BINDING sequence T description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 55) chain A residue 482 type BINDING sequence T description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 56) chain A residue 661 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 57) chain D residue 482 type BINDING sequence T description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 58) chain D residue 661 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 59) chain D residue 662 type BINDING sequence S description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 60) chain C residue 662 type BINDING sequence S description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 61) chain A residue 662 type BINDING sequence S description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 62) chain B residue 482 type BINDING sequence T description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 63) chain B residue 661 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 64) chain B residue 662 type BINDING sequence S description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 65) chain C residue 661 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 66) chain B residue 667 type SITE sequence F description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 67) chain B residue 759 type SITE sequence L description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 68) chain C residue 455 type SITE sequence A description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 69) chain C residue 667 type SITE sequence F description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 70) chain C residue 759 type SITE sequence L description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 71) chain D residue 455 type SITE sequence A description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 72) chain D residue 667 type SITE sequence F description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 73) chain D residue 759 type SITE sequence L description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 74) chain A residue 455 type SITE sequence A description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 75) chain A residue 667 type SITE sequence F description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 76) chain A residue 759 type SITE sequence L description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 77) chain B residue 455 type SITE sequence A description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 78) chain A residue 640 type SITE sequence S description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 79) chain B residue 640 type SITE sequence S description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 80) chain C residue 640 type SITE sequence S description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 81) chain D residue 640 type SITE sequence S description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 82) chain A residue 669 type MOD_RES sequence K description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 83) chain B residue 669 type MOD_RES sequence K description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 84) chain C residue 669 type MOD_RES sequence K description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 85) chain D residue 669 type MOD_RES sequence K description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 86) chain A residue 703 type MOD_RES sequence L description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 87) chain B residue 703 type MOD_RES sequence L description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 88) chain C residue 703 type MOD_RES sequence L description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 89) chain D residue 703 type MOD_RES sequence L description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13

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