eF-site ID 3c1b-ABCDEFGH
PDB Code 3c1b
Chain A, B, C, D, E, F, G, H

click to enlarge
Title The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure
Classification Structural PROTEIN/DNA
Compound Histone H3-like
Source Xenopus laevis (African clawed frog) (3C1B)
Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPKDIQLARRIRGERA
B:  RDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFL
ENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLPKK
D:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF
ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA
VSEGTKAVTKYTSAK
E:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ
DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR
VTIMPKDIQLARRIRGERA
F:  KRHRXVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR
GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR
TLYGFGG
G:  TRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVL
EYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNK
LLGRVTIAQGGVLPNIQSVLLPK
H:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF
ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA
VSEGTKAVTKYTSA
Description


Functional site

1) chain C
residue 821-827
type prosite
sequence AGLQFPV
description HISTONE_H2A Histone H2A signature. AGLqFPV
source prosite : PS00046

2) chain D
residue 1289-1311
type prosite
sequence REIQTAVRLLLPGELAKHAVSEG
description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
source prosite : PS00357

3) chain A
residue 466-474
type prosite
sequence PFQRLVREI
description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
source prosite : PS00959

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

5) chain F
residue 259
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI10

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

7) chain F
residue 277
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI11

8) chain E
residue 656
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI11

9) chain E
residue 679
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI11

10) 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

11) chain F
residue 231
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

12) chain A
residue 480
type CROSSLNK
sequence T
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI13

13) 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

14) chain A
residue 507
type CROSSLNK
sequence T
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI13

15) chain F
residue 291
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

16) chain A
residue 515
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI14

17) chain E
residue 715
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI14

18) chain A
residue 522
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI15

19) chain E
residue 722
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI15

20) chain E
residue 637
type MOD_RES
sequence K
description N6-methyllysine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI19

21) chain A
residue 486
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI20

22) chain E
residue 686
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI20

23) chain A
residue 510
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI21

24) chain E
residue 710
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI21

25) chain C
residue 895
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI3

26) chain G
residue 1095
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI3

27) chain C
residue 836
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI4

28) chain G
residue 1036
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI4

29) chain C
residue 874
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

30) chain C
residue 875
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

31) chain G
residue 1074
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

32) chain G
residue 1075
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

33) chain F
residue 216
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

34) chain F
residue 244
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

35) chain F
residue 279
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

36) chain C
residue 904
type MOD_RES
sequence Q
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

37) chain G
residue 1104
type MOD_RES
sequence Q
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

38) chain F
residue 220
type MOD_RES
sequence X
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

39) chain C
residue 918
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

40) chain G
residue 1118
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

41) chain F
residue 231
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

42) chain F
residue 291
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

43) chain F
residue 247
type CROSSLNK
sequence S
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

44) chain C
residue 815
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

45) chain C
residue 919
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

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

47) chain E
residue 664
type MOD_RES
sequence K
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9

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

49) chain F
residue 251
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9

50) chain F
residue 288
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9

51) chain A
residue 464
type MOD_RES
sequence K
description Phosphotyrosine => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI9


Display surface

Download
Links