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

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Title Crystal Structure of Human Nucleosome Core Particle Containing H3K122Q mutation
Classification STRUCTURAL PROTEIN/DNA
Compound Histone H3.1
Source Homo sapiens (Human) (3AZH)
Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRV
TIMPQDIQLARRIRGER
B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN
VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
C:  KAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLA
AVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEE
LNKLLGRVTIAQGGVLPNIQAVLLPK
D:  KRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDI
FERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKH
AVSEGTKAVTKYTSA
E:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ
DFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKR
VTIMPQDIQLARRIRGERA
F:  HRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGV
LKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTL
YGFG
G:  KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAV
LEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN
KLLGRVTIAQGGVLPNIQAVLLPK
H:  RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER
IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS
EGTKAVTKYTSA
Description


Functional site

1) chain C
residue 45
type
sequence A
description BINDING SITE FOR RESIDUE CL C 1001
source : AC1

2) chain C
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE CL C 1001
source : AC1

3) chain C
residue 47
type
sequence A
description BINDING SITE FOR RESIDUE CL C 1001
source : AC1

4) chain D
residue 91
type
sequence S
description BINDING SITE FOR RESIDUE CL C 1001
source : AC1

5) chain D
residue 48
type
sequence V
description BINDING SITE FOR RESIDUE MN D 201
source : AC2

6) chain E
residue 76
type
sequence Q
description BINDING SITE FOR RESIDUE MN D 201
source : AC2

7) chain E
residue 77
type
sequence D
description BINDING SITE FOR RESIDUE MN D 201
source : AC2

8) chain E
residue 121
type
sequence P
description BINDING SITE FOR RESIDUE CL E 1001
source : AC3

9) chain E
residue 122
type
sequence Q
description BINDING SITE FOR RESIDUE CL E 1001
source : AC3

10) chain G
residue 44
type
sequence G
description BINDING SITE FOR RESIDUE CL G 1001
source : AC4

11) chain G
residue 45
type
sequence A
description BINDING SITE FOR RESIDUE CL G 1001
source : AC4

12) chain G
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE CL G 1001
source : AC4

13) chain H
residue 90
type
sequence T
description BINDING SITE FOR RESIDUE CL G 1001
source : AC4

14) chain H
residue 91
type
sequence S
description BINDING SITE FOR RESIDUE CL G 1001
source : AC4

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

16) chain D
residue 92-114
type prosite
sequence REIQTAVRLLLPGELAKHAVSEG
description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
source prosite : PS00357

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

18) chain D
residue 36
type MOD_RES
sequence S
description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475
source Swiss-Prot : SWS_FT_FI10

19) chain H
residue 36
type MOD_RES
sequence S
description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475
source Swiss-Prot : SWS_FT_FI10

20) chain E
residue 56
type MOD_RES
sequence K
description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475
source Swiss-Prot : SWS_FT_FI10

21) chain D
residue 46
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
source Swiss-Prot : SWS_FT_FI11

22) chain D
residue 108
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
source Swiss-Prot : SWS_FT_FI11

23) chain H
residue 46
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
source Swiss-Prot : SWS_FT_FI11

24) chain H
residue 108
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
source Swiss-Prot : SWS_FT_FI11

25) chain D
residue 57
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
source Swiss-Prot : SWS_FT_FI12

26) chain H
residue 57
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
source Swiss-Prot : SWS_FT_FI12

27) chain D
residue 79
type MOD_RES
sequence R
description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
source Swiss-Prot : SWS_FT_FI13

28) chain H
residue 79
type MOD_RES
sequence R
description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
source Swiss-Prot : SWS_FT_FI13

29) chain D
residue 86
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
source Swiss-Prot : SWS_FT_FI14

30) chain D
residue 92
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
source Swiss-Prot : SWS_FT_FI14

31) chain H
residue 86
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
source Swiss-Prot : SWS_FT_FI14

32) chain H
residue 92
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
source Swiss-Prot : SWS_FT_FI14

33) chain D
residue 115
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q00729
source Swiss-Prot : SWS_FT_FI15

34) chain H
residue 115
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q00729
source Swiss-Prot : SWS_FT_FI15

35) chain F
residue 91
type MOD_RES
sequence K
description Phosphothreonine => ECO:0000250|UniProtKB:Q00729
source Swiss-Prot : SWS_FT_FI15

36) chain D
residue 112
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI16

37) chain H
residue 112
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI16

38) chain B
residue 79
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI16

39) chain F
residue 20
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI16

40) chain F
residue 59
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI16

41) chain F
residue 79
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
source Swiss-Prot : SWS_FT_FI16

42) chain D
residue 120
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563
source Swiss-Prot : SWS_FT_FI18

43) chain H
residue 120
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563
source Swiss-Prot : SWS_FT_FI18

44) chain D
residue 34
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
source Swiss-Prot : SWS_FT_FI20

45) chain H
residue 34
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
source Swiss-Prot : SWS_FT_FI20

46) chain A
residue 79
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
source Swiss-Prot : SWS_FT_FI21

47) chain E
residue 79
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
source Swiss-Prot : SWS_FT_FI21

48) chain A
residue 80
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:20850016
source Swiss-Prot : SWS_FT_FI22

49) chain E
residue 80
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:20850016
source Swiss-Prot : SWS_FT_FI22

50) chain A
residue 86
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI23

51) chain E
residue 86
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P84243
source Swiss-Prot : SWS_FT_FI23

52) chain A
residue 107
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI24

53) chain E
residue 107
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI24

54) chain A
residue 115
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
source Swiss-Prot : SWS_FT_FI25

55) chain E
residue 115
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
source Swiss-Prot : SWS_FT_FI25

56) chain A
residue 122
type MOD_RES
sequence Q
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
source Swiss-Prot : SWS_FT_FI26

57) chain E
residue 122
type MOD_RES
sequence Q
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
source Swiss-Prot : SWS_FT_FI26

58) chain H
residue 43
type MOD_RES
sequence K
description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
source Swiss-Prot : SWS_FT_FI3

59) chain H
residue 85
type MOD_RES
sequence K
description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
source Swiss-Prot : SWS_FT_FI3

60) chain D
residue 43
type MOD_RES
sequence K
description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
source Swiss-Prot : SWS_FT_FI3

61) chain D
residue 85
type MOD_RES
sequence K
description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
source Swiss-Prot : SWS_FT_FI3

62) chain G
residue 95
type MOD_RES
sequence K
description ADP-ribosylserine => ECO:0000269|PubMed:34874266
source Swiss-Prot : SWS_FT_FI4

63) chain B
residue 44
type MOD_RES
sequence K
description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
source Swiss-Prot : SWS_FT_FI5

64) chain F
residue 44
type MOD_RES
sequence K
description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
source Swiss-Prot : SWS_FT_FI5

65) chain B
residue 77
type MOD_RES
sequence K
description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711
source Swiss-Prot : SWS_FT_FI6

66) chain B
residue 91
type MOD_RES
sequence K
description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711
source Swiss-Prot : SWS_FT_FI6

67) chain F
residue 31
type MOD_RES
sequence K
description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711
source Swiss-Prot : SWS_FT_FI6

68) chain F
residue 77
type MOD_RES
sequence K
description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711
source Swiss-Prot : SWS_FT_FI6

69) chain F
residue 91
type MOD_RES
sequence K
description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711
source Swiss-Prot : SWS_FT_FI6

70) chain G
residue 74
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
source Swiss-Prot : SWS_FT_FI7

71) chain G
residue 75
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
source Swiss-Prot : SWS_FT_FI7

72) chain D
residue 34
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

73) chain D
residue 116
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

74) chain D
residue 120
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

75) chain H
residue 34
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

76) chain H
residue 116
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

77) chain H
residue 120
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

78) chain D
residue 35
type MOD_RES
sequence E
description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
source Swiss-Prot : SWS_FT_FI9

79) chain H
residue 35
type MOD_RES
sequence E
description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
source Swiss-Prot : SWS_FT_FI9

80) chain G
residue 118
type MOD_RES
sequence K
description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
source Swiss-Prot : SWS_FT_FI9


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