eF-site ID 3b6f-ABCDEFGHIJ
PDB Code 3b6f
Chain A, B, C, D, E, F, G, H, I, J

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Title Nucleosome core particle treated with cisplatin
Classification STRUCTURAL PROTEIN/DNA
Compound 147-MER DNA
Source Xenopus laevis (African clawed frog) (3B6F)
Sequence A:  GGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVR
EIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAI
HAKRVTIMPKDIQLARRIRGERA
B:  DNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLE
NVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
C:  KTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAV
LEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELN
KLLGRVTIAQGGVLPNIQSVLLPKKT
D:  DGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNS
FVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPG
ELAKHAVSEGTKAVTKYTSAK
E:  ATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRL
VREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLC
AIHAKRVTIMPKDIQLARRIRGERA
F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR
GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR
TLYGFGG
G:  KAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLA
AVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEE
LNKLLGRVTIAQGGVLPNIQSVLLPKKTE
H:  KKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFV
NDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGEL
AKHAVSEGTKAVTKYTSAK
I:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG
AAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGC
TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT
TGGTAGTATCTGCAGGTGGATATTGAT
J:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG
AAACTGCTCCATCAAAAGGCATGTTCAGCTGGATTCCAGC
TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT
TGGTAGTATCTGCAGGTGGATATTGAT
Description


Functional site

1) chain C
residue 64
type
sequence E
description BINDING SITE FOR RESIDUE MN E 3132
source : AC1

2) chain D
residue 45
type
sequence V
description BINDING SITE FOR RESIDUE MN E 3132
source : AC1

3) chain E
residue 76
type
sequence Q
description BINDING SITE FOR RESIDUE MN E 3132
source : AC1

4) chain E
residue 77
type
sequence D
description BINDING SITE FOR RESIDUE MN E 3132
source : AC1

5) chain A
residue 37
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

6) 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

7) 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

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

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

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

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

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

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

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

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

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

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

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

19) chain A
residue 36
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI10

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

21) chain E
residue 36
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI10

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

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

24) 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

25) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

40) 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

41) 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

42) chain H
residue 117
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI4

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

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

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

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

47) chain F
residue 16
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

48) chain F
residue 44
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

49) chain F
residue 79
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

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

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

52) chain F
residue 20
type MOD_RES
sequence K
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

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

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

55) chain F
residue 31
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

56) chain F
residue 91
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

57) chain F
residue 47
type CROSSLNK
sequence S
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

58) 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

59) 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

60) chain G
residue 13
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

61) 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

62) 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

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

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

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

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

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

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

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


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