eF-site ID 4u1x-ABCD PDB Code 4u1x Chain A, B, C, D click to enlarge Title Full length GluA2-kainate-(R,R)-2b complex crystal form B Classification Transport protein, Membrane protein Compound Glutamate receptor 2 Source (GRIA2_RAT) Sequence A:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR KIGYWSEVDKMVVTLTEDDTSGLEQKTVVVTTILESPYVM MKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGD GKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREE VIDFSKPFMSLGISIMIKKPQKFSFLDPLAYEIWMAIVFA YILVSVVLFLVSPRSLSARIVAGVWWFFTLIIISSYTANL AAFLTVERMSPIESAEDLSKQTEIAYGTLDSGSTKEFFRR SKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYA YLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSS LGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKSALSL SNVAGVFYILVGGLGLAMLVALI B:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR KIGYWSEVDKMVVTLTEDDLEQKTVVVTTILESPYVMMKK NHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKY GARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVID FSKPFMSLGISIMIKKPQKSKPGVPLAYEIWMAIVFAYIL VSVVLFLVARIVAGVWWFFTLIIISSYTANLAAFLTVERM VSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDK MWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMN EYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLA VLKLSEQGVLDKLKNKWWYDKGECGAKALSLSNVAGVFYI LVGGLGLAMLVALIEFAY C:  SIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNL EVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCG TLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQW DKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINN DKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVIT IGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDY DDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQ VMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIE RALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRK IGYWSEVDKMVVTLTELEQKTVVVTTILESPYVMMKKNHE MLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGAR DADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSK PFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMAIVFAY ILVSVVLFLVSRFPRSLSARIVAGVWWFFTLIIISSYTAN LAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFF RRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGK YAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKG SSLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSG SKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEF D:  IQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLE VANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGT LHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWD KFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINND KKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITI GKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDYD DSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQV MTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIER ALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKI GYWSEVDKMVVTLTELEQKTVVVTTILESPYVMMKKNHEM LEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARD ADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKP FMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMAIVFAYI LVSVVLFLVSPRSLSARIVAGVWWFFTLIIISSYTANLAA FLTVMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKI AVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLL ESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGT PVNLAVLKLSEQGVLDKLKNKWWYDKGECGEKTSALSLSN VAGVFYILVGGLGLAMLVALIEFA Description Functional site 1) chain A residue 593 type LIPID sequence P description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 2) chain C residue 593 type LIPID sequence P description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 3) chain D residue 593 type LIPID sequence P description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 4) chain A residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 5) chain B residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 6) chain C residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 7) chain D residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 8) chain A residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 9) chain B residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 10) chain C residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 11) chain D residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 12) chain A residue 594-599 type TOPO_DOM sequence RSLSAR description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 13) chain C residue 594-599 type TOPO_DOM sequence RSLSAR description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 14) chain D residue 594-599 type TOPO_DOM sequence RSLSAR description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 15) chain A residue 621-795 type TOPO_DOM sequence AAFLTVERMSPIESAEDLSKQTEIAYGTLDSGSTKEFFRR SKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYA YLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSS LGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKSALSL SNVAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 16) chain B residue 621-795 type TOPO_DOM sequence AAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFR RSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKY AYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS SLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKALSL SNVAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 17) chain C residue 621-795 type TOPO_DOM sequence AAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFR RSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKY AYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS SLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGS KEKTSALSLSNVAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 18) chain D residue 621-795 type TOPO_DOM sequence AAFLTVMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRS KIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAY LLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSL GTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGEKTSALSL SNVAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 19) chain B residue 796-816 type TRANSMEM sequence FYILVGGLGLAMLVALIEFAY description Helical; Name=M4 source Swiss-Prot : SWS_FT_FI6 20) chain A residue 457 type SITE sequence T description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 21) chain D residue 457 type SITE sequence T description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 22) chain D residue 664 type SITE sequence I description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 23) chain D residue 756 type SITE sequence Q description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 24) chain A residue 664 type SITE sequence I description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 25) chain A residue 756 type SITE sequence Q description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 26) chain B residue 457 type SITE sequence T description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 27) chain B residue 664 type SITE sequence I description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 28) chain B residue 756 type SITE sequence Q description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 29) chain C residue 457 type SITE sequence T description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 30) chain C residue 664 type SITE sequence I description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 31) chain C residue 756 type SITE sequence Q description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI10 32) chain A residue 637 type SITE sequence E description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 33) chain B residue 637 type SITE sequence E description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 34) chain C residue 637 type SITE sequence E description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 35) chain D residue 637 type SITE sequence E description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI11 36) chain A residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 37) chain B residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 38) chain C residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 39) chain D residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 40) chain A residue 353 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 41) chain B residue 353 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 42) chain C residue 353 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 43) chain D residue 353 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 44) chain A residue 389 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 45) chain A residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 46) chain B residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 47) chain C residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 48) chain D residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 49) chain A residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 50) chain B residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 51) chain C residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 52) chain D residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 53) chain A residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 54) chain D residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 55) chain D residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 56) chain D residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 57) chain A residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 58) chain A residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 59) chain B residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 60) chain B residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 61) chain B residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 62) chain C residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 63) chain C residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 64) chain C residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 65) chain A residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 66) chain B residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 67) chain C residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 68) chain D residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 69) chain A residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 70) chain D residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 71) chain D residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 72) chain D residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 73) chain A residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 74) chain A residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 75) chain B residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 76) chain B residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 77) chain B residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 78) chain C residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 79) chain C residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 80) chain C residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9

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