eF-site ID 3lz0-ABCDEFGH
PDB Code 3lz0
Chain A, B, C, D, E, F, G, H

click to enlarge
Title Crystal Structure of Nucleosome Core Particle Composed of the Widom 601 DNA Sequence (orientation 1)
Classification STRUCTURAL PROTEIN/DNA
Compound Histone H3.2
Source Xenopus laevis (African clawed frog) (3LZ0)
Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPKDIQLARRIRGER
B:  KVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYG
FGG
C:  TRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVL
EYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNK
LLGRVTIAQGGVLPNIQSVLLPK
D:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF
ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA
VSEGTKAVTKYTSAK
E:  HRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDF
KTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVT
IMPKDIQLARRIRGERA
F:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN
VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLPK
H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE
RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV
SEGTKAVTKYTSA
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 C
residue 44
type
sequence G
description BINDING SITE FOR RESIDUE CL C 1101
source : AC9

4) chain C
residue 45
type
sequence A
description BINDING SITE FOR RESIDUE CL C 1101
source : AC9

5) chain C
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE CL C 1101
source : AC9

6) chain D
residue 87
type
sequence T
description BINDING SITE FOR RESIDUE CL C 1101
source : AC9

7) chain D
residue 88
type
sequence S
description BINDING SITE FOR RESIDUE CL C 1101
source : AC9

8) chain G
residue 44
type
sequence G
description BINDING SITE FOR RESIDUE CL G 1102
source : BC1

9) chain G
residue 45
type
sequence A
description BINDING SITE FOR RESIDUE CL G 1102
source : BC1

10) chain G
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE CL G 1102
source : BC1

11) chain G
residue 47
type
sequence A
description BINDING SITE FOR RESIDUE CL G 1102
source : BC1

12) chain H
residue 87
type
sequence T
description BINDING SITE FOR RESIDUE CL G 1102
source : BC1

13) chain H
residue 88
type
sequence S
description BINDING SITE FOR RESIDUE CL G 1102
source : BC1

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

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

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

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

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

19) chain F
residue 59
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 B
residue 77
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI11

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

23) 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

24) 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

25) 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

26) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

47) chain D
residue 109
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI3

48) chain H
residue 109
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI3

49) chain D
residue 117
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4
source Swiss-Prot : SWS_FT_FI4

50) chain H
residue 117
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4
source Swiss-Prot : SWS_FT_FI4

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


Display surface

Download
Links