eF-site ID 1p3f-ABCDEFGH
PDB Code 1p3f
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) (1P3F)
Sequence A:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ
DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR
VTIMPKDIQLARRIRGERA
B:  RDNIQGITKPAIRRLARRGGVKCISGLIYEETRGVLKVFL
ENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
C:  KTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAV
LEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELN
KLLGRVTIAQGGVLPNIQSVLLPK
D:  ESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIA
GEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEG
TKAVTKYTSAK
E:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ
DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR
VTIMPKDIQLARRIRGERA
F:  VLRDNIQGITKPAIRRLARRGGVKCISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF
GG
G:  KAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLA
AVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEE
LNKLLGRVTIAQGGVLPNIQSVLLPKK
H:  KSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF
ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA
VSEGTKAVTKYTSAK
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

23) 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

24) 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

25) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

39) 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

40) 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

41) 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

42) 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

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

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

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

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

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

48) chain E
residue 664
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI10

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

50) chain A
residue 437
type MOD_RES
sequence K
description N6-methyllysine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI13

51) chain E
residue 637
type MOD_RES
sequence K
description N6-methyllysine => ECO:0000250|UniProtKB:P68431
source Swiss-Prot : SWS_FT_FI13

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


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