eF-site ID 5jiy-ABFG
PDB Code 5jiy
Chain A, B, F, G

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Title Structure of G9a SET-domain with Histone H3K9norLeucine mutant peptide and bound S-adenosylmethionine
Classification TRANSFERASE
Compound Histone-lysine N-methyltransferase EHMT2
Source Homo sapiens (Human) (5JIY)
Sequence A:  IRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISE
NCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCW
YDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSG
IKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDA
EADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLC
DPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG
DRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSR
B:  EKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCE
TSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDK
DGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKV
RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEAD
VREDDSYLFDLDEVYCIDARYYGNISRFINHLCDPNIIPV
RVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIK
SKYFTCQCGSEKCKHSAEAIALEQSRL
F:  KQTARXST
G:  TKQTARXST
Description


Functional site

1) chain A
residue 974
type
sequence C
description binding site for residue ZN A 1201
source : AC1

2) chain A
residue 987
type
sequence C
description binding site for residue ZN A 1201
source : AC1

3) chain A
residue 1017
type
sequence C
description binding site for residue ZN A 1201
source : AC1

4) chain A
residue 1021
type
sequence C
description binding site for residue ZN A 1201
source : AC1

5) chain A
residue 974
type
sequence C
description binding site for residue ZN A 1202
source : AC2

6) chain A
residue 976
type
sequence C
description binding site for residue ZN A 1202
source : AC2

7) chain A
residue 980
type
sequence C
description binding site for residue ZN A 1202
source : AC2

8) chain A
residue 985
type
sequence C
description binding site for residue ZN A 1202
source : AC2

9) chain A
residue 980
type
sequence C
description binding site for residue ZN A 1203
source : AC3

10) chain A
residue 1017
type
sequence C
description binding site for residue ZN A 1203
source : AC3

11) chain A
residue 1023
type
sequence C
description binding site for residue ZN A 1203
source : AC3

12) chain A
residue 1027
type
sequence C
description binding site for residue ZN A 1203
source : AC3

13) chain A
residue 1115
type
sequence C
description binding site for residue ZN A 1204
source : AC4

14) chain A
residue 1168
type
sequence C
description binding site for residue ZN A 1204
source : AC4

15) chain A
residue 1170
type
sequence C
description binding site for residue ZN A 1204
source : AC4

16) chain A
residue 1175
type
sequence C
description binding site for residue ZN A 1204
source : AC4

17) chain A
residue 1048
type
sequence M
description binding site for residue SAM A 1205
source : AC5

18) chain A
residue 1050
type
sequence W
description binding site for residue SAM A 1205
source : AC5

19) chain A
residue 1084
type
sequence S
description binding site for residue SAM A 1205
source : AC5

20) chain A
residue 1085
type
sequence Y
description binding site for residue SAM A 1205
source : AC5

21) chain A
residue 1109
type
sequence R
description binding site for residue SAM A 1205
source : AC5

22) chain A
residue 1110
type
sequence F
description binding site for residue SAM A 1205
source : AC5

23) chain A
residue 1111
type
sequence I
description binding site for residue SAM A 1205
source : AC5

24) chain A
residue 1112
type
sequence N
description binding site for residue SAM A 1205
source : AC5

25) chain A
residue 1113
type
sequence H
description binding site for residue SAM A 1205
source : AC5

26) chain A
residue 1154
type
sequence Y
description binding site for residue SAM A 1205
source : AC5

27) chain A
residue 1158
type
sequence F
description binding site for residue SAM A 1205
source : AC5

28) chain A
residue 1166
type
sequence F
description binding site for residue SAM A 1205
source : AC5

29) chain A
residue 1167
type
sequence T
description binding site for residue SAM A 1205
source : AC5

30) chain A
residue 1168
type
sequence C
description binding site for residue SAM A 1205
source : AC5

31) chain A
residue 1169
type
sequence Q
description binding site for residue SAM A 1205
source : AC5

32) chain F
residue 9
type
sequence X
description binding site for residue SAM A 1205
source : AC5

33) chain B
residue 974
type
sequence C
description binding site for residue ZN B 1201
source : AC6

34) chain B
residue 987
type
sequence C
description binding site for residue ZN B 1201
source : AC6

35) chain B
residue 1017
type
sequence C
description binding site for residue ZN B 1201
source : AC6

36) chain B
residue 1021
type
sequence C
description binding site for residue ZN B 1201
source : AC6

37) chain B
residue 980
type
sequence C
description binding site for residue ZN B 1202
source : AC7

38) chain B
residue 1017
type
sequence C
description binding site for residue ZN B 1202
source : AC7

39) chain B
residue 1023
type
sequence C
description binding site for residue ZN B 1202
source : AC7

40) chain B
residue 1027
type
sequence C
description binding site for residue ZN B 1202
source : AC7

41) chain B
residue 974
type
sequence C
description binding site for residue ZN B 1203
source : AC8

42) chain B
residue 976
type
sequence C
description binding site for residue ZN B 1203
source : AC8

43) chain B
residue 980
type
sequence C
description binding site for residue ZN B 1203
source : AC8

44) chain B
residue 985
type
sequence C
description binding site for residue ZN B 1203
source : AC8

45) chain B
residue 1115
type
sequence C
description binding site for residue ZN B 1204
source : AC9

46) chain B
residue 1168
type
sequence C
description binding site for residue ZN B 1204
source : AC9

47) chain B
residue 1170
type
sequence C
description binding site for residue ZN B 1204
source : AC9

48) chain B
residue 1175
type
sequence C
description binding site for residue ZN B 1204
source : AC9

49) chain B
residue 1048
type
sequence M
description binding site for residue SAM B 1205
source : AD1

50) chain B
residue 1050
type
sequence W
description binding site for residue SAM B 1205
source : AD1

51) chain B
residue 1084
type
sequence S
description binding site for residue SAM B 1205
source : AD1

52) chain B
residue 1085
type
sequence Y
description binding site for residue SAM B 1205
source : AD1

53) chain B
residue 1109
type
sequence R
description binding site for residue SAM B 1205
source : AD1

54) chain B
residue 1110
type
sequence F
description binding site for residue SAM B 1205
source : AD1

55) chain B
residue 1112
type
sequence N
description binding site for residue SAM B 1205
source : AD1

56) chain B
residue 1113
type
sequence H
description binding site for residue SAM B 1205
source : AD1

57) chain B
residue 1154
type
sequence Y
description binding site for residue SAM B 1205
source : AD1

58) chain B
residue 1166
type
sequence F
description binding site for residue SAM B 1205
source : AD1

59) chain B
residue 1167
type
sequence T
description binding site for residue SAM B 1205
source : AD1

60) chain B
residue 1168
type
sequence C
description binding site for residue SAM B 1205
source : AD1

61) chain B
residue 1169
type
sequence Q
description binding site for residue SAM B 1205
source : AD1

62) chain A
residue 1082
type MOD_RES
sequence D
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

63) chain A
residue 1119
type MOD_RES
sequence I
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 1146
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

65) chain A
residue 1149
type MOD_RES
sequence E
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

66) chain B
residue 1008
type MOD_RES
sequence K
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

67) chain B
residue 1010
type MOD_RES
sequence E
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

68) chain B
residue 1014
type MOD_RES
sequence I
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

69) chain B
residue 1019
type MOD_RES
sequence Q
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

70) chain B
residue 1021
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

71) chain B
residue 1051
type MOD_RES
sequence G
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

72) chain G
residue 3
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

73) chain B
residue 1055
type MOD_RES
sequence L
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

74) chain B
residue 1057
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

75) chain B
residue 1061
type MOD_RES
sequence G
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

76) chain B
residue 1082
type MOD_RES
sequence D
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

77) chain B
residue 1119
type MOD_RES
sequence I
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

78) chain B
residue 1146
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

79) chain B
residue 1149
type MOD_RES
sequence E
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

80) chain A
residue 1014
type MOD_RES
sequence I
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

81) chain A
residue 1019
type MOD_RES
sequence Q
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

82) chain A
residue 1021
type MOD_RES
sequence C
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

83) chain A
residue 1051
type MOD_RES
sequence G
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

84) chain A
residue 1055
type MOD_RES
sequence L
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

85) chain A
residue 1057
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

86) chain A
residue 1061
type MOD_RES
sequence G
description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
source Swiss-Prot : SWS_FT_FI1

87) chain F
residue 4
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI2

88) chain G
residue 4
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI2

89) chain F
residue 5
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI3

90) chain G
residue 5
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI3

91) chain F
residue 6
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI4

92) chain G
residue 6
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI4

93) chain F
residue 8
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI5

94) chain G
residue 8
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI5

95) chain F
residue 9
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI6

96) chain G
residue 9
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI6

97) chain F
residue 10
type MOD_RES
sequence S
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
source Swiss-Prot : SWS_FT_FI7

98) chain G
residue 10
type MOD_RES
sequence S
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
source Swiss-Prot : SWS_FT_FI7

99) chain F
residue 11
type MOD_RES
sequence T
description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
source Swiss-Prot : SWS_FT_FI8

100) chain G
residue 11
type MOD_RES
sequence T
description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
source Swiss-Prot : SWS_FT_FI8


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