eF-site ID 5b1l-ABCDEFGHIJ
PDB Code 5b1l
Chain A, B, C, D, E, F, G, H, I, J

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Title The mouse nucleosome structure containing H3t
Classification STRUCTURAL PROTEIN/DNA
Compound Histone H3t
Source (5B1L)
Sequence A:  PHRYHPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEACESYLVGLFEDTNLCAIHAKRV
TIMPKDIQLARRIRGER
B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN
VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
C:  RAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVY
LAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRND
EELNKLLGRVTIAQGGVLPNIQAVLLPK
D:  GRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFE
RIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAV
SEGTKAVTKYTSS
E:  PHRYHPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEACESYLVGLFEDTNLCAIHAKRV
TIMPKDIQLARRIRGER
F:  RKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVL
KVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLY
GFGG
G:  KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAV
LEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN
KLLGRVTIAQGGVLPNIQAVLLPK
H:  RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER
IASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVS
EGTKAVTKYTSS
I:  TCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGA
AACTGCTCCATCAAAAGGCATGTTCAGCTGAATTCAGCTG
AACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTG
GTAGAATCTGCAGGTGGATATTGAT
J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG
AAACTGCTCCATCAAAAGGCATGTTCAGCTGAATTCAGCT
GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT
GGTAGAATCTGCAGGTGGATATTGA
Description


Functional site

1) chain A
residue 121
type
sequence P
description binding site for residue CL A 301
source : AC1

2) chain A
residue 122
type
sequence K
description binding site for residue CL A 301
source : AC1

3) chain C
residue 44
type
sequence G
description binding site for residue CL C 301
source : AC2

4) chain C
residue 46
type
sequence G
description binding site for residue CL C 301
source : AC2

5) chain C
residue 47
type
sequence A
description binding site for residue CL C 301
source : AC2

6) chain D
residue 90
type
sequence T
description binding site for residue CL C 301
source : AC2

7) chain D
residue 91
type
sequence S
description binding site for residue CL C 301
source : AC2

8) chain D
residue 48
type
sequence V
description binding site for residue MN D 301
source : AC3

9) chain E
residue 77
type
sequence D
description binding site for residue MN D 301
source : AC3

10) chain E
residue 121
type
sequence P
description binding site for residue CL E 301
source : AC4

11) chain E
residue 122
type
sequence K
description binding site for residue CL E 301
source : AC4

12) chain G
residue 44
type
sequence G
description binding site for residue CL G 301
source : AC5

13) chain G
residue 46
type
sequence G
description binding site for residue CL G 301
source : AC5

14) chain G
residue 47
type
sequence A
description binding site for residue CL G 301
source : AC5

15) chain H
residue 91
type
sequence S
description binding site for residue CL G 301
source : AC5

16) chain I
residue 121
type
sequence G
description binding site for residue MN I 301
source : AC6

17) chain I
residue 134
type
sequence G
description binding site for residue MN I 303
source : AC8

18) chain I
residue 68
type
sequence G
description binding site for residue MN I 304
source : AC9

19) chain I
residue 17
type
sequence A
description binding site for residue MN I 306
source : AD2

20) chain J
residue 267
type
sequence G
description binding site for residue MN J 401
source : AD3

21) chain J
residue 185
type
sequence G
description binding site for residue MN J 402
source : AD4

22) chain J
residue 186
type
sequence G
description binding site for residue MN J 402
source : AD4

23) chain J
residue 280
type
sequence G
description binding site for residue MN J 403
source : AD5

24) chain J
residue 183
type
sequence T
description binding site for residue MN J 404
source : AD6

25) chain J
residue 217
type
sequence G
description binding site for residue MN J 405
source : AD7

26) chain A
residue 122
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI10

27) chain E
residue 122
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI10

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

29) chain D
residue 92-114
type prosite
sequence REVQTAVRLLLPGELAKHAVSEG
description HISTONE_H2B Histone H2B signature. REVQTavRlLLpGELaKHAVSEG
source prosite : PS00357

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

31) chain A
residue 57
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI18

32) chain E
residue 57
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI18

33) chain A
residue 80
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI19

34) chain E
residue 80
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI19

35) chain A
residue 86
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI20

36) chain E
residue 86
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI20

37) chain H
residue 120
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI20

38) chain A
residue 107
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI21

39) chain E
residue 107
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI21

40) chain A
residue 115
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI22

41) chain E
residue 115
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI22

42) chain A
residue 128
type MOD_RES
sequence R
description Phosphoarginine => ECO:0000305
source Swiss-Prot : SWS_FT_FI23

43) chain A
residue 129
type MOD_RES
sequence R
description Phosphoarginine => ECO:0000305
source Swiss-Prot : SWS_FT_FI23

44) chain E
residue 128
type MOD_RES
sequence R
description Phosphoarginine => ECO:0000305
source Swiss-Prot : SWS_FT_FI23

45) chain E
residue 129
type MOD_RES
sequence R
description Phosphoarginine => ECO:0000305
source Swiss-Prot : SWS_FT_FI23

46) chain A
residue 131
type MOD_RES
sequence R
description Phosphoarginine => ECO:0000255
source Swiss-Prot : SWS_FT_FI24

47) chain E
residue 131
type MOD_RES
sequence R
description Phosphoarginine => ECO:0000255
source Swiss-Prot : SWS_FT_FI24

48) chain A
residue 64
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI15

49) chain E
residue 64
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI15

50) chain F
residue 20
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI15

51) chain F
residue 59
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI15

52) chain F
residue 79
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI15

53) chain A
residue 41
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI16

54) chain E
residue 41
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI16

55) chain F
residue 91
type MOD_RES
sequence K
description Phosphotyrosine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI16

56) chain A
residue 56
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI17

57) chain A
residue 79
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI17

58) chain E
residue 56
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI17

59) chain E
residue 79
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI17

60) chain H
residue 85
type MOD_RES
sequence K
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

61) chain D
residue 85
type MOD_RES
sequence K
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

62) chain B
residue 44
type MOD_RES
sequence K
description Phosphothreonine; by PKC => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI5

63) chain F
residue 44
type MOD_RES
sequence K
description Phosphothreonine; by PKC => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI5

64) chain G
residue 74
type MOD_RES
sequence K
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000269|PubMed:15485929
source Swiss-Prot : SWS_FT_FI6

65) chain G
residue 75
type MOD_RES
sequence K
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000269|PubMed:15485929
source Swiss-Prot : SWS_FT_FI6

66) chain G
residue 118
type MOD_RES
sequence K
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105
source Swiss-Prot : SWS_FT_FI8

67) chain H
residue 34
type MOD_RES
sequence K
description Phosphothreonine; by PKC and CHEK1 => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI9

68) chain H
residue 116
type MOD_RES
sequence K
description Phosphothreonine; by PKC and CHEK1 => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI9


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