eF-site ID 2nzd-ABCDEFGH
PDB Code 2nzd
Chain A, B, C, D, E, F, G, H

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Title Nucleosome core particle containing 145 bp of DNA
Classification STRUCTURAL PROTEIN/DNA
Compound DNA (145-MER)
Source Xenopus laevis (African clawed frog) (2NZD)
Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPKDIQLARRIRGER
B:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF
GG
C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLPKK
D:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF
ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA
VSEGTKAVTKYTSAK
E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPKDIQLARRIRGER
F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR
GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR
TLYGFGG
G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLPKK
H:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF
ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA
VSEGTKAVTKYTSAK
Description


Functional site

1) chain D
residue 45
type
sequence V
description BINDING SITE FOR RESIDUE MN E 1001
source : AC1

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

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

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

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

6) chain E
residue 64
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI10

7) chain A
residue 64
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI10

8) chain F
residue 92
type MOD_RES
sequence R
description N6-methyllysine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI13

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

29) chain C
residue 95
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI3

30) chain G
residue 95
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI3

31) chain C
residue 36
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI4

32) chain G
residue 36
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI4

33) chain H
residue 118
type MOD_RES
sequence Y
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI4

34) chain C
residue 74
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

35) chain C
residue 75
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

36) chain G
residue 74
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

37) chain G
residue 75
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

38) chain F
residue 17
type MOD_RES
sequence R
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

39) chain F
residue 45
type MOD_RES
sequence R
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

40) chain F
residue 80
type MOD_RES
sequence T
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

41) chain C
residue 104
type MOD_RES
sequence Q
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

42) chain G
residue 104
type MOD_RES
sequence Q
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

43) chain F
residue 21
type MOD_RES
sequence V
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

44) chain C
residue 118
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

45) chain G
residue 118
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

46) chain F
residue 32
type MOD_RES
sequence P
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

47) chain F
residue 92
type MOD_RES
sequence R
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

48) chain C
residue 15
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

49) chain C
residue 119
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

50) chain G
residue 15
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

51) chain G
residue 119
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

52) chain F
residue 52
type MOD_RES
sequence E
description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI9

53) chain F
residue 89
type MOD_RES
sequence A
description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI9


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