eF-site ID 3rel-ABCDEFGHIJ
PDB Code 3rel
Chain A, B, C, D, E, F, G, H, I, J

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Title 2.7 Angstrom Crystal Structure of the Nucleosome Core Particle Assembled with a 146 bp Alpha-Satellite DNA (NCP146b) Derivatized with Triamminechloroplatinum(II) Chloride
Classification STRUCTURAL PROTEIN/DNA
Compound Histone H3.2
Source Xenopus laevis (African clawed frog) (3REL)
Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPKDIQLARRIRGERA
B:  KVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYG
FGG
C:  TRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVL
EYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNK
LLGRVTIAQGGVLPNIQSVLLPK
D:  KKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFV
NDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGEL
AKHAVSEGTKAVTKYTSAK
E:  HRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDF
KTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVT
IMPKDIQLARRIRGERA
F:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN
VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLPK
H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE
RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV
SEGTKAVTKYTSAK
I:  ATCTCCAAATATCCCTTGCGGATCGTAGAAAAAGTGTGTC
AAACTGCGCTATCAAAGGGAAACTTCAACTGAATTCAGTT
GAAGTTTCCCTTTGATAGCGCAGTTTGACACACTTTTTCT
ACGATCCGCAAGGGATATTTGGAGAT
J:  ATCTCCAAATATCCCTTGCGGATCGTAGAAAAAGTGTGTC
AAACTGCGCTATCAAAGGGAAACTTCAACTGAATTCAGTT
GAAGTTTCCCTTTGATAGCGCAGTTTGACACACTTTTTCT
ACGATCCGCAAGGGATATTTGGAGAT
Description


Functional site

1) chain A
residue 77
type
sequence D
description BINDING SITE FOR RESIDUE MN A 1001
source : AC1

2) chain H
residue 45
type
sequence V
description BINDING SITE FOR RESIDUE MN A 1001
source : AC1

3) chain D
residue 45
type
sequence V
description BINDING SITE FOR RESIDUE MN D 1007
source : AC2

4) chain C
residue 71
type
sequence R
description BINDING SITE FOR RESIDUE SO4 D 1101
source : AC3

5) chain D
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE SO4 D 1101
source : AC3

6) chain D
residue 47
type
sequence P
description BINDING SITE FOR RESIDUE SO4 D 1101
source : AC3

7) chain D
residue 48
type
sequence D
description BINDING SITE FOR RESIDUE SO4 D 1101
source : AC3

8) chain D
residue 49
type
sequence T
description BINDING SITE FOR RESIDUE SO4 D 1101
source : AC3

9) chain C
residue 45
type
sequence A
description BINDING SITE FOR RESIDUE SO4 C 1102
source : AC4

10) chain C
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE SO4 C 1102
source : AC4

11) chain C
residue 47
type
sequence A
description BINDING SITE FOR RESIDUE SO4 C 1102
source : AC4

12) chain D
residue 87
type
sequence T
description BINDING SITE FOR RESIDUE SO4 C 1102
source : AC4

13) chain D
residue 88
type
sequence S
description BINDING SITE FOR RESIDUE SO4 C 1102
source : AC4

14) chain G
residue 44
type
sequence G
description BINDING SITE FOR RESIDUE SO4 G 1103
source : AC5

15) chain G
residue 45
type
sequence A
description BINDING SITE FOR RESIDUE SO4 G 1103
source : AC5

16) chain G
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE SO4 G 1103
source : AC5

17) chain G
residue 47
type
sequence A
description BINDING SITE FOR RESIDUE SO4 G 1103
source : AC5

18) chain H
residue 87
type
sequence T
description BINDING SITE FOR RESIDUE SO4 G 1103
source : AC5

19) chain H
residue 88
type
sequence S
description BINDING SITE FOR RESIDUE SO4 G 1103
source : AC5

20) chain J
residue 7
type
sequence G
description BINDING SITE FOR RESIDUE PT J 73
source : AC6

21) chain J
residue 68
type
sequence G
description BINDING SITE FOR RESIDUE PT J 74
source : AC7

22) chain J
residue 58
type
sequence G
description BINDING SITE FOR RESIDUE PT J 75
source : AC8

23) chain J
residue -3
type
sequence G
description BINDING SITE FOR RESIDUE PT J 76
source : AC9

24) chain J
residue -2
type
sequence A
description BINDING SITE FOR RESIDUE PT J 76
source : AC9

25) chain I
residue -14
type
sequence G
description BINDING SITE FOR RESIDUE PT I 74
source : BC1

26) chain I
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE PT I 75
source : BC2

27) chain J
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE PT J 77
source : BC3

28) chain I
residue 5
type
sequence G
description BINDING SITE FOR RESIDUE PT I 76
source : BC4

29) chain J
residue 4
type
sequence G
description BINDING SITE FOR RESIDUE PT J 78
source : BC5

30) chain I
residue 59
type
sequence G
description BINDING SITE FOR RESIDUE PT I 77
source : BC6

31) chain I
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE PT I 77
source : BC6

32) chain J
residue -46
type
sequence G
description BINDING SITE FOR RESIDUE PT J 79
source : BC7

33) chain I
residue -53
type
sequence G
description BINDING SITE FOR RESIDUE PT I 78
source : BC8

34) chain I
residue 68
type
sequence G
description BINDING SITE FOR RESIDUE PT I 79
source : BC9

35) chain I
residue 69
type
sequence G
description BINDING SITE FOR RESIDUE PT I 79
source : BC9

36) chain I
residue 58
type
sequence A
description BINDING SITE FOR RESIDUE PT I 80
source : CC1

37) chain I
residue 59
type
sequence G
description BINDING SITE FOR RESIDUE PT I 80
source : CC1

38) chain I
residue -72
type
sequence A
description BINDING SITE FOR RESIDUE PT I 81
source : CC2

39) chain I
residue -45
type
sequence G
description BINDING SITE FOR RESIDUE PT I 82
source : CC3

40) chain J
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE PT J 80
source : CC4

41) chain I
residue -16
type
sequence G
description BINDING SITE FOR RESIDUE PT I 83
source : CC5

42) chain J
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE PT J 81
source : CC6

43) chain J
residue 70
type
sequence G
description BINDING SITE FOR RESIDUE PT J 82
source : CC7

44) chain I
residue 27
type
sequence G
description BINDING SITE FOR RESIDUE PT I 84
source : CC8

45) chain J
residue -40
type
sequence G
description BINDING SITE FOR RESIDUE PT J 83
source : CC9

46) chain I
residue -15
type
sequence G
description BINDING SITE FOR RESIDUE PT I 85
source : DC1

47) chain I
residue 25
type
sequence G
description BINDING SITE FOR RESIDUE PT I 86
source : DC2

48) chain I
residue 33
type
sequence T
description BINDING SITE FOR RESIDUE PT I 87
source : DC3

49) chain I
residue 34
type
sequence G
description BINDING SITE FOR RESIDUE PT I 87
source : DC3

50) chain J
residue -73
type
sequence A
description BINDING SITE FOR RESIDUE PT J 84
source : DC4

51) chain J
residue -55
type
sequence C
description BINDING SITE FOR RESIDUE PT J 85
source : DC5

52) chain I
residue -55
type
sequence G
description BINDING SITE FOR RESIDUE PT I 88
source : DC6

53) chain J
residue 59
type
sequence G
description BINDING SITE FOR RESIDUE PT J 86
source : DC7

54) chain J
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE PT J 86
source : DC7

55) chain J
residue -18
type
sequence A
description BINDING SITE FOR RESIDUE PT J 87
source : DC8

56) chain J
residue -17
type
sequence G
description BINDING SITE FOR RESIDUE PT J 87
source : DC8

57) chain F
residue 84
type
sequence M
description BINDING SITE FOR RESIDUE PT F 103
source : DC9

58) chain B
residue 84
type
sequence M
description BINDING SITE FOR RESIDUE PT B 103
source : EC1

59) chain I
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE PT I 89
source : EC2

60) chain I
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE PT I 90
source : EC3

61) chain I
residue 61
type
sequence G
description BINDING SITE FOR RESIDUE PT I 90
source : EC3

62) chain J
residue -15
type
sequence G
description BINDING SITE FOR RESIDUE PT J 88
source : EC4

63) chain I
residue 3
type
sequence C
description BINDING SITE FOR RESIDUE PT I 91
source : EC5

64) chain I
residue 4
type
sequence A
description BINDING SITE FOR RESIDUE PT I 91
source : EC5

65) chain J
residue -16
type
sequence G
description BINDING SITE FOR RESIDUE PT J 89
source : EC6

66) chain J
residue -17
type
sequence G
description BINDING SITE FOR RESIDUE PT J 89
source : EC6

67) chain J
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE PT J 90
source : EC7

68) chain J
residue 68
type
sequence G
description BINDING SITE FOR RESIDUE PT J 90
source : EC7

69) chain J
residue 24
type
sequence G
description BINDING SITE FOR RESIDUE PT J 92
source : EC9

70) chain J
residue 25
type
sequence C
description BINDING SITE FOR RESIDUE PT J 92
source : EC9

71) chain J
residue -54
type
sequence G
description BINDING SITE FOR RESIDUE PT J 93
source : FC1

72) chain I
residue -46
type
sequence A
description BINDING SITE FOR RESIDUE PT I 93
source : FC2

73) chain I
residue -35
type
sequence G
description BINDING SITE FOR RESIDUE PT I 94
source : FC3

74) chain I
residue -35
type
sequence G
description BINDING SITE FOR RESIDUE PT I 95
source : FC4

75) chain I
residue -2
type
sequence G
description BINDING SITE FOR RESIDUE PT I 96
source : FC5

76) chain I
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE PT I 97
source : FC6

77) chain J
residue -36
type
sequence G
description BINDING SITE FOR RESIDUE PT J 106
source : FC7

78) chain B
residue 59
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI10

79) chain E
residue 64
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI10

80) chain F
residue 59
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI10

81) chain A
residue 64
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI10

82) chain B
residue 77
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI11

83) chain F
residue 77
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI11

84) chain B
residue 31
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI12

85) chain F
residue 31
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI12

86) chain B
residue 91
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI13

87) chain F
residue 91
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI13

88) chain A
residue 41
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI14

89) chain E
residue 41
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI14

90) chain A
residue 56
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

91) chain A
residue 79
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

92) chain E
residue 56
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

93) chain E
residue 79
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

94) chain A
residue 57
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI16

95) chain E
residue 57
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI16

96) chain A
residue 80
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

97) chain A
residue 107
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

98) chain E
residue 80
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

99) chain E
residue 107
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

100) chain B
residue 51
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9

101) chain B
residue 88
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9

102) chain F
residue 51
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9

103) chain F
residue 88
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9

104) chain A
residue 86
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI18

105) chain E
residue 86
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI18

106) chain A
residue 115
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI19

107) chain E
residue 115
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI19

108) chain A
residue 122
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI20

109) chain E
residue 122
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI20

110) chain A
residue 110
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI21

111) chain E
residue 110
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI21

112) chain H
residue 117
type MOD_RES
sequence K
description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI4

113) chain C
residue 21-27
type prosite
sequence AGLQFPV
description HISTONE_H2A Histone H2A signature. AGLqFPV
source prosite : PS00046

114) chain A
residue 66-74
type prosite
sequence PFQRLVREI
description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
source prosite : PS00959

115) chain D
residue 89-111
type prosite
sequence REIQTAVRLLLPGELAKHAVSEG
description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
source prosite : PS00357

116) chain G
residue 95
type MOD_RES
sequence K
description Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI3

117) chain B
residue 44
type MOD_RES
sequence K
description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI5

118) chain B
residue 79
type MOD_RES
sequence K
description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI5

119) chain F
residue 44
type MOD_RES
sequence K
description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI5

120) chain F
residue 79
type MOD_RES
sequence K
description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI5

121) chain B
residue 20
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI6

122) chain B
residue 31
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI7

123) chain B
residue 91
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI7

124) chain F
residue 31
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI7

125) chain F
residue 91
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI7

126) chain B
residue 47
type MOD_RES
sequence S
description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI8

127) chain F
residue 47
type MOD_RES
sequence S
description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI8

128) chain G
residue 15
type MOD_RES
sequence K
description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI8


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