eF-site ID 4u4g-ABCD
PDB Code 4u4g
Chain A, B, C, D

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Title Structure of GluA2* in complex with competitive antagonist ZK 200775
Classification TRANSPORT PROTEIN
Compound Glutamate receptor 2
Source (GRIA2_RAT)
Sequence A:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN
LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC
GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ
WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN
NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI
TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD
YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV
QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI
ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR
KIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK
KNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK
YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI
DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCI
VFAYIGVSVVLFLVSTNEFGIFNSLWFSLGAFMQPRSLSG
RIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAED
LSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAE
PSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPC
DTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGV
LDKLKNKWWYDKGECSALSLSNVAGVFYILVGGLGLAMLV
ALIEFCYK
B:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN
LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC
GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ
WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN
NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI
TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD
YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV
QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI
ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR
KIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK
KNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK
YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI
DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCI
VFAYIGVSVVLFLVSTNEFGIFNSLWFSLGAFMQPRSLSG
RIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAED
LSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAE
PSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPC
DTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGV
LDKLKNKWWYDKGECSALSLSNVAGVFYILVGGLGLAMLV
ALIEFCYK
C:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN
LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC
GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ
WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN
NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI
TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD
YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV
QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI
ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR
KIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK
KNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK
YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI
DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCI
VFAYIGVSVVLFLVSTNEFGIFNSLWFSLGAFMQPRSLSG
RIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAED
LSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAE
PSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPC
DTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGV
LDKLKNKWWYDKGECSALSLSNVAGVFYILVGGLGLAMLV
ALIEFCYK
D:  NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDN
LEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC
GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQ
WDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN
NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVI
TIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD
YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAV
QVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI
ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPR
KIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK
KNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK
YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI
DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCI
VFAYIGVSVVLFLVSTNEFGIFNSLWFSLGAFMQPRSLSG
RIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAED
LSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAE
PSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPC
DTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGV
LDKLKNKWWYDKGECSALSLSNVAGVFYILVGGLGLAMLV
ALIEFCYK
Description


Functional site

1) chain A
residue 355
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

2) chain B
residue 355
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

3) chain C
residue 355
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

4) chain D
residue 355
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

5) chain A
residue 391
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

6) chain A
residue 398
type CARBOHYD
sequence T
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

7) chain B
residue 391
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

8) chain B
residue 398
type CARBOHYD
sequence T
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

9) chain C
residue 391
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

10) chain C
residue 398
type CARBOHYD
sequence T
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

11) chain D
residue 391
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

12) chain D
residue 398
type CARBOHYD
sequence T
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI17

13) chain A
residue 668
type MOD_RES
sequence D
description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI12

14) chain B
residue 668
type MOD_RES
sequence D
description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI12

15) chain C
residue 668
type MOD_RES
sequence D
description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI12

16) chain D
residue 668
type MOD_RES
sequence D
description Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI12

17) chain A
residue 702
type MOD_RES
sequence Y
description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI13

18) chain B
residue 702
type MOD_RES
sequence Y
description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI13

19) chain C
residue 702
type MOD_RES
sequence Y
description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI13

20) chain D
residue 702
type MOD_RES
sequence Y
description Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
source Swiss-Prot : SWS_FT_FI13

21) chain A
residue 595
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI14

22) chain B
residue 595
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI14

23) chain C
residue 595
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI14

24) chain D
residue 595
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI14

25) chain A
residue 456
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

26) chain D
residue 456
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

27) chain D
residue 491
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

28) chain D
residue 711
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

29) chain A
residue 491
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

30) chain A
residue 711
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

31) chain B
residue 456
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

32) chain B
residue 491
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

33) chain B
residue 711
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

34) chain C
residue 456
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

35) chain C
residue 491
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

36) chain C
residue 711
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:16483599
source Swiss-Prot : SWS_FT_FI7

37) chain A
residue 484
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI8

38) chain B
residue 484
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI8

39) chain C
residue 484
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI8

40) chain D
residue 484
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI8

41) chain A
residue 486
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

42) chain D
residue 486
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

43) chain D
residue 660
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

44) chain D
residue 661
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

45) chain A
residue 660
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

46) chain A
residue 661
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

47) chain B
residue 486
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

48) chain B
residue 660
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

49) chain B
residue 661
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

50) chain C
residue 486
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

51) chain C
residue 660
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

52) chain C
residue 661
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI9

53) chain A
residue 241
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873
source Swiss-Prot : SWS_FT_FI15

54) chain B
residue 241
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873
source Swiss-Prot : SWS_FT_FI15

55) chain C
residue 241
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873
source Swiss-Prot : SWS_FT_FI15

56) chain D
residue 241
type CARBOHYD
sequence E
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873
source Swiss-Prot : SWS_FT_FI15

57) chain A
residue 459
type SITE
sequence I
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

58) chain D
residue 459
type SITE
sequence I
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

59) chain D
residue 666
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

60) chain D
residue 758
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

61) chain A
residue 666
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

62) chain A
residue 758
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

63) chain B
residue 459
type SITE
sequence I
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

64) chain B
residue 666
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

65) chain B
residue 758
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

66) chain C
residue 459
type SITE
sequence I
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

67) chain C
residue 666
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

68) chain C
residue 758
type SITE
sequence V
description Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI10

69) chain A
residue 639
type SITE
sequence L
description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI11

70) chain B
residue 639
type SITE
sequence L
description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI11

71) chain C
residue 639
type SITE
sequence L
description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI11

72) chain D
residue 639
type SITE
sequence L
description Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
source Swiss-Prot : SWS_FT_FI11

73) chain A
residue 602-622
type TRANSMEM
sequence GGVWWFFTLIIISSYTANLAA
description Helical
source Swiss-Prot : SWS_FT_FI1

74) chain B
residue 602-622
type TRANSMEM
sequence GGVWWFFTLIIISSYTANLAA
description Helical
source Swiss-Prot : SWS_FT_FI1

75) chain C
residue 602-622
type TRANSMEM
sequence GGVWWFFTLIIISSYTANLAA
description Helical
source Swiss-Prot : SWS_FT_FI1

76) chain D
residue 602-622
type TRANSMEM
sequence GGVWWFFTLIIISSYTANLAA
description Helical
source Swiss-Prot : SWS_FT_FI1

77) chain A
residue 596-601
type TOPO_DOM
sequence LSGRIV
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI2

78) chain B
residue 596-601
type TOPO_DOM
sequence LSGRIV
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI2

79) chain C
residue 596-601
type TOPO_DOM
sequence LSGRIV
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI2

80) chain D
residue 596-601
type TOPO_DOM
sequence LSGRIV
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI2

81) chain A
residue 593-595
type INTRAMEM
sequence PRS
description
source Swiss-Prot : SWS_FT_FI4

82) chain B
residue 593-595
type INTRAMEM
sequence PRS
description
source Swiss-Prot : SWS_FT_FI4

83) chain C
residue 593-595
type INTRAMEM
sequence PRS
description
source Swiss-Prot : SWS_FT_FI4

84) chain D
residue 593-595
type INTRAMEM
sequence PRS
description
source Swiss-Prot : SWS_FT_FI4

85) chain A
residue 623-797
type TOPO_DOM
sequence FLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRS
KIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAY
LLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSL
GTPVNLAVLKLSEQGVLDKLKNKWWYDKGECSALSLSNVA
GVFY
description Extracellular
source Swiss-Prot : SWS_FT_FI5

86) chain B
residue 623-797
type TOPO_DOM
sequence FLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRS
KIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAY
LLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSL
GTPVNLAVLKLSEQGVLDKLKNKWWYDKGECSALSLSNVA
GVFY
description Extracellular
source Swiss-Prot : SWS_FT_FI5

87) chain C
residue 623-797
type TOPO_DOM
sequence FLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRS
KIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAY
LLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSL
GTPVNLAVLKLSEQGVLDKLKNKWWYDKGECSALSLSNVA
GVFY
description Extracellular
source Swiss-Prot : SWS_FT_FI5

88) chain D
residue 623-797
type TOPO_DOM
sequence FLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRS
KIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAY
LLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSL
GTPVNLAVLKLSEQGVLDKLKNKWWYDKGECSALSLSNVA
GVFY
description Extracellular
source Swiss-Prot : SWS_FT_FI5


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