eF-site ID 3c33-AB
PDB Code 3c33
Chain A, B

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Title Crystal structure of GluR5 ligand-binding core in complex with potassium at 1.78 Angstrom resolution
Classification MEMBRANE PROTEIN
Compound GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 1
Source Rattus norvegicus (Rat) (GRIK1_RAT)
Sequence A:  RTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKEL
SNILGFLYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRAD
LAVAPLTITYVREKVIDFSKPFMTLGISILYRKGTPIDSA
DDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSS
RQQSALVKNSDEGIQRVLTTDYALLMESTSIEYVTQRNCN
LTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKL
HMMKEKWWRGNGCP
B:  RTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKEL
SNILGFLYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRAD
LAVAPLTITYVREKVIDFSKPFMTLGISILYRKGTPIDSA
DDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSS
RQQSALVKNSDEGIQRVLTTDYALLMESTSIEYVTQRNCN
LTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKL
HMMKEKWWRGNGCP
Description


Functional site

1) chain B
residue 96
type
sequence E
description BINDING SITE FOR RESIDUE K B 301
source : AC1

2) chain B
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE K B 301
source : AC1

3) chain B
residue 100
type
sequence D
description BINDING SITE FOR RESIDUE K B 301
source : AC1

4) chain A
residue 96
type
sequence E
description BINDING SITE FOR RESIDUE K A 302
source : AC2

5) chain A
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE K A 302
source : AC2

6) chain A
residue 100
type
sequence D
description BINDING SITE FOR RESIDUE K A 302
source : AC2

7) chain A
residue 181
type
sequence L
description BINDING SITE FOR RESIDUE K B 303
source : AC3

8) chain B
residue 22
type
sequence S
description BINDING SITE FOR RESIDUE K B 303
source : AC3

9) chain A
residue 103
type
sequence K
description BINDING SITE FOR RESIDUE CL A 304
source : AC4

10) chain A
residue 227
type
sequence R
description BINDING SITE FOR RESIDUE CL A 304
source : AC4

11) chain B
residue 103
type
sequence K
description BINDING SITE FOR RESIDUE CL A 304
source : AC4

12) chain A
residue 31
type
sequence R
description BINDING SITE FOR RESIDUE CL A 305
source : AC5

13) chain A
residue 54
type
sequence K
description BINDING SITE FOR RESIDUE CL A 305
source : AC5

14) chain A
residue 55
type
sequence L
description BINDING SITE FOR RESIDUE CL A 305
source : AC5

15) chain B
residue 20
type
sequence R
description BINDING SITE FOR RESIDUE CL B 306
source : AC6

16) chain B
residue 22
type
sequence S
description BINDING SITE FOR RESIDUE CL B 306
source : AC6

17) chain B
residue 31
type
sequence R
description BINDING SITE FOR RESIDUE CL B 307
source : AC7

18) chain B
residue 54
type
sequence K
description BINDING SITE FOR RESIDUE CL B 307
source : AC7

19) chain B
residue 55
type
sequence L
description BINDING SITE FOR RESIDUE CL B 307
source : AC7

20) chain A
residue 13
type
sequence E
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

21) chain A
residue 61
type
sequence Y
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

22) chain A
residue 88
type
sequence P
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

23) chain A
residue 90
type
sequence T
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

24) chain A
residue 95
type
sequence R
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

25) chain A
residue 140
type
sequence G
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

26) chain A
residue 141
type
sequence S
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

27) chain A
residue 142
type
sequence T
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

28) chain A
residue 190
type
sequence E
description BINDING SITE FOR RESIDUE KAI A 401
source : AC8

29) chain B
residue 13
type
sequence E
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

30) chain B
residue 61
type
sequence Y
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

31) chain B
residue 88
type
sequence P
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

32) chain B
residue 90
type
sequence T
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

33) chain B
residue 95
type
sequence R
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

34) chain B
residue 140
type
sequence G
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

35) chain B
residue 141
type
sequence S
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

36) chain B
residue 142
type
sequence T
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

37) chain B
residue 190
type
sequence E
description BINDING SITE FOR RESIDUE KAI B 401
source : AC9

38) chain B
residue 60
type
sequence K
description BINDING SITE FOR RESIDUE GOL B 402
source : BC1

39) chain B
residue 61
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 402
source : BC1

40) chain B
residue 62
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 402
source : BC1

41) chain B
residue 63
type
sequence A
description BINDING SITE FOR RESIDUE GOL B 402
source : BC1

42) chain B
residue 138
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 402
source : BC1

43) chain B
residue 139
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 402
source : BC1

44) chain A
residue 60
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 402
source : BC2

45) chain A
residue 61
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 402
source : BC2

46) chain A
residue 62
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 402
source : BC2

47) chain A
residue 63
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 402
source : BC2

48) chain A
residue 138
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 402
source : BC2

49) chain A
residue 139
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 402
source : BC2

50) chain A
residue 213
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

51) chain A
residue 214
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

52) chain B
residue 104
type
sequence P
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

53) chain B
residue 105
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

54) chain B
residue 106
type
sequence M
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

55) chain B
residue 107
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

56) chain B
residue 238
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

57) chain B
residue 243
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 403
source : BC3

58) chain B
residue 13
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 403
source : BC4

59) chain B
residue 14
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 403
source : BC4

60) chain B
residue 174
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 403
source : BC4

61) chain B
residue 189
type
sequence M
description BINDING SITE FOR RESIDUE GOL B 403
source : BC4

62) chain B
residue 193
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 403
source : BC4

63) chain B
residue 196
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 403
source : BC4

64) chain A
residue 88
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

65) chain A
residue 90
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

66) chain A
residue 141
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

67) chain A
residue 142
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

68) chain B
residue 88
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

69) chain B
residue 90
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

70) chain B
residue 141
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

71) chain B
residue 142
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI1

72) chain A
residue 95
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI2

73) chain A
residue 190
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI2

74) chain B
residue 95
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI2

75) chain B
residue 190
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240, ECO:0007744|PDB:1YCJ
source Swiss-Prot : SWS_FT_FI2

76) chain A
residue 162
type MOD_RES
sequence S
description Phosphoserine; by PKC => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

77) chain B
residue 162
type MOD_RES
sequence S
description Phosphoserine; by PKC => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

78) chain A
residue 198
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

79) chain B
residue 198
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

80) chain A
residue 203
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI5

81) chain B
residue 203
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI5


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