eF-site ID 1p3g-ABCDEFGH
PDB Code 1p3g
Chain A, B, C, D, E, F, G, H

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Title Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
Classification STRUCTURAL PROTEIN/DNA
Compound Palindromic 146bp Human Alpha-Satellite DNA fragment
Source Xenopus laevis (African clawed frog) (1P3G)
Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPKDIQLARRIRGERA
B:  DNIQGITKPAIRRLARRGGVKEISGLIYEETRGVLKVFLE
NVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLP
D:  RKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFER
IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS
EGTKAVTKYTSAK
E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPKDIQLARRIRGERA
F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKEISGLIYEETR
GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR
TLYGFGG
G:  AKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYL
AAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDE
ELNKLLGRVTIAQGGVLPNIQSVLLPKK
H:  KESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERI
AGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSE
GTKAVTKYTSAK
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 E
residue 664
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI10

5) chain A
residue 464
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI10

6) chain F
residue 292
type MOD_RES
sequence R
description N6-methyllysine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI13

7) chain A
residue 441
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI14

8) chain E
residue 641
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI14

9) chain A
residue 456
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

10) chain A
residue 479
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

11) chain E
residue 656
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

12) chain E
residue 679
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI15

13) chain A
residue 457
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI16

14) chain E
residue 657
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI16

15) chain A
residue 480
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

16) chain A
residue 507
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

17) chain E
residue 680
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

18) chain E
residue 707
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI17

19) chain A
residue 486
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI18

20) chain E
residue 686
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI18

21) chain A
residue 515
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI19

22) chain E
residue 715
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI19

23) chain A
residue 522
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI20

24) chain E
residue 722
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI20

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

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

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

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

29) 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

30) 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

31) chain H
residue 1518
type MOD_RES
sequence Y
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI4

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

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

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

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

36) chain F
residue 217
type MOD_RES
sequence R
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

37) chain F
residue 245
type MOD_RES
sequence E
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

38) chain F
residue 280
type MOD_RES
sequence T
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

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

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

41) chain F
residue 221
type MOD_RES
sequence V
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

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

43) chain F
residue 232
type MOD_RES
sequence P
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

44) chain F
residue 292
type MOD_RES
sequence R
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI7

45) 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

46) chain G
residue 1013
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

47) chain G
residue 1015
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

48) chain G
residue 1119
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 F
residue 252
type MOD_RES
sequence E
description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI9

50) chain F
residue 289
type MOD_RES
sequence A
description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
source Swiss-Prot : SWS_FT_FI9


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