eF-site ID 4u1w-ABCD PDB Code 4u1w Chain A, B, C, D click to enlarge Title Full length GluA2-kainate-(R,R)-2b complex crystal form A Classification Transport protein, Membrane protein Compound Glutamate receptor 2 Source (GRIA2_RAT) Sequence A:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNKE RRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTD GDLLKIQFGGAEVSGFQIVDYDDSLVSKFIERWSTLEEKE YPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRR GNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQ NGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTEDEQ KTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEI AKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKA DIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKP GVFSFLDPLAYEIWMAIVFAYIGVSVVLFLVSSLSARIVA GVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQ TEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVF VRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMK VGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGVLDKL KNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGG LGLAMLVALIE B:  SIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNL EVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCG TLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQW DKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINN DKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVIT IGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDY DDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQ VMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIE RALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRK IGYWSEVDKMVVTLTEQKTVVVTTILESPYVMMKKNHEML EGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDA DTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPF MSLGISIMIKKPQKSKPGVFSFLDPLIWMAIVFAYIGVSV VLFLVSPRSLSARIVAGVWWFFTLIIISSYTANLAAFLTV ERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAV FDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLES TMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPV NLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSKEKTSA LSLSNVAGVFYILVGGLGLAMLVALIEFAYK C:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR KIGYWSEVDKMVVTLTEDDTSGLKTVVVTTILESPYVMMK KNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKVFSFLDPLAYEIWMAIVFAYIGV SVVLFLVLSARIVAGVWWFFTLIIISSYTANLAAFLTVER MVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFD KMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTM NEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNL AVLKLSEQGVLDKLKNKWWYDKGECGALSLSNVAGVFYIL VGGLGLAMLVALIEFA D:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR KIGYWSEVDKMVVTLTEDDTSGLEQKTVVVTTILESPYVM MKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGD GKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREE VIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWM AIVFAYIGVSVVLFLVSLSARIVAGVWWFFTLIIISSYTA NLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEF FRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKG KYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPK GSSLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGATSA LSLSNVAGVFYILVGGLGLAMLVALIEFAY Description Functional site 1) chain A residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 2) chain B residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 3) chain C residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 4) chain D residue 600-620 type TRANSMEM sequence IVAGVWWFFTLIIISSYTANL description Helical source Swiss-Prot : SWS_FT_FI1 5) 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 6) 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 7) 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 8) 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 9) chain A residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 10) chain B residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 11) chain C residue 389 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 12) chain C residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 13) chain D residue 389 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 14) chain D residue 396 type CARBOHYD sequence V description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI17 15) chain A residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 16) chain B residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 17) chain C residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 18) chain D residue 666 type MOD_RES sequence V description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI12 19) chain A residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 20) chain B residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 21) chain C residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 22) chain D residue 700 type MOD_RES sequence Y description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 source Swiss-Prot : SWS_FT_FI13 23) chain B residue 593 type LIPID sequence P description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 24) chain A residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 25) chain B residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 26) chain C residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 27) chain D residue 239 type CARBOHYD sequence E description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 source Swiss-Prot : SWS_FT_FI15 28) chain A residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 29) chain D residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 30) chain D residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 31) chain D residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 32) chain A residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 34) chain B residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 35) chain B residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 36) chain B residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 37) chain C residue 454 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 38) chain C residue 489 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 39) chain C residue 709 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16483599 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 41) chain B residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 42) chain C residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 43) chain D residue 482 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI8 44) chain A residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 45) chain D residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 46) chain D residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 47) chain D residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 48) chain A residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 49) chain A residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 50) chain B residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 51) chain B residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 52) chain B residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 53) chain C residue 484 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 54) chain C residue 658 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 55) chain C residue 659 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25103405 source Swiss-Prot : SWS_FT_FI9 56) chain B residue 594-599 type TOPO_DOM sequence RSLSAR description Cytoplasmic source Swiss-Prot : SWS_FT_FI2 57) chain A residue 621-795 type TOPO_DOM sequence AAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFR RSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKY AYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS SLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGS KEKTSALSLSNVAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 58) chain B residue 621-795 type TOPO_DOM sequence AAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFR RSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKY AYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS SLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGS KEKTSALSLSNVAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 59) chain C residue 621-795 type TOPO_DOM sequence AAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFR RSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKY AYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS SLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGALSLSN VAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 60) chain D residue 621-795 type TOPO_DOM sequence AAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFR RSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKY AYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS SLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGATSALS LSNVAGV description Extracellular source Swiss-Prot : SWS_FT_FI5 61) chain B residue 796-816 type TRANSMEM sequence FYILVGGLGLAMLVALIEFAY description Helical; Name=M4 source Swiss-Prot : SWS_FT_FI6 62) chain D residue 796-816 type TRANSMEM sequence FYILVGGLGLAMLVALIEFAY description Helical; Name=M4 source Swiss-Prot : SWS_FT_FI6 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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

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