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5B1M

The mouse nucleosome structure containing H3.1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0043505cellular_componentCENP-A containing nucleosome
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006325biological_processchromatin organization
C0030527molecular_functionstructural constituent of chromatin
C0031492molecular_functionnucleosomal DNA binding
C0043505cellular_componentCENP-A containing nucleosome
C0046982molecular_functionprotein heterodimerization activity
C0061644biological_processprotein localization to CENP-A containing chromatin
C0070828biological_processheterochromatin organization
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0043505cellular_componentCENP-A containing nucleosome
F0046982molecular_functionprotein heterodimerization activity
F0061644biological_processprotein localization to CENP-A containing chromatin
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0006325biological_processchromatin organization
G0030527molecular_functionstructural constituent of chromatin
G0031492molecular_functionnucleosomal DNA binding
G0043505cellular_componentCENP-A containing nucleosome
G0046982molecular_functionprotein heterodimerization activity
G0061644biological_processprotein localization to CENP-A containing chromatin
G0070828biological_processheterochromatin organization
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REVQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG92-GLY114

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylproline => ECO:0000250|UniProtKB:P23527
ChainResidueDetails
DPRO1
HPRO1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: ADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DGLU2
HGLU2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: ADP-ribosylserine => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DSER6
HSER6

site_idSWS_FT_FI4
Number of Residues10
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
DLYS11
HLYS85
DLYS15
DLYS16
DLYS20
DLYS85
HLYS11
HLYS15
HLYS16
HLYS20

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
ChainResidueDetails
DLYS12
HLYS12
BLYS44
FLYS8
FLYS16
FLYS44

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583
ChainResidueDetails
DSER14
HSER14
GLYS74
GLYS75

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DLYS23
DLYS43
HLYS23
HLYS43
ELYS27
ELYS36

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS24
HLYS24
CLYS125
GLYS118
GLYS119
GLYS125

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DLYS34
DLYS116
HLYS34
HLYS116

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:32822587
ChainResidueDetails
DGLU35
HGLU35
GLYS13
GLYS15

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000269|PubMed:20647423, ECO:0000269|PubMed:32822587
ChainResidueDetails
DSER36
HSER36
GLYS119

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DLYS46
DLYS108
HLYS46
HLYS108

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS57
HLYS57

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG79
HARG79

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG86
DARG92
HARG86
HARG92
FLYS12
FLYS20
FLYS59
FLYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DTHR115
HTHR115
FLYS91

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
DLYS120
HLYS120
ELYS56
ELYS79

site_idSWS_FT_FI18
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DSER112
HSER112

site_idSWS_FT_FI19
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6
ChainResidueDetails
DLYS20
HLYS20

site_idSWS_FT_FI20
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62808
ChainResidueDetails
ASER86
DLYS120
HLYS120

site_idSWS_FT_FI21
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DLYS34
HLYS34

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI23
Number of Residues4
DetailsMOD_RES: Phosphoarginine => ECO:0000305
ChainResidueDetails
AARG128
AARG129
EARG128
EARG129

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphoarginine => ECO:0000255
ChainResidueDetails
AARG131
EARG131

site_idSWS_FT_FI25
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ALYS18
ELYS18

218853

PDB entries from 2024-04-24

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