Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ZBB

Structure of the 4_601_167 Tetranucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
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
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
a0000786cellular_componentnucleosome
a0003677molecular_functionDNA binding
a0005515molecular_functionprotein binding
a0005634cellular_componentnucleus
a0005654cellular_componentnucleoplasm
a0005694cellular_componentchromosome
a0030527molecular_functionstructural constituent of chromatin
a0046982molecular_functionprotein heterodimerization activity
b0000786cellular_componentnucleosome
b0003677molecular_functionDNA binding
b0005515molecular_functionprotein binding
b0005634cellular_componentnucleus
b0005694cellular_componentchromosome
b0006334biological_processnucleosome assembly
b0030527molecular_functionstructural constituent of chromatin
b0046982molecular_functionprotein heterodimerization activity
c0000786cellular_componentnucleosome
c0003677molecular_functionDNA binding
c0005634cellular_componentnucleus
c0005694cellular_componentchromosome
c0030527molecular_functionstructural constituent of chromatin
c0031507biological_processheterochromatin formation
c0046982molecular_functionprotein heterodimerization activity
d0000786cellular_componentnucleosome
d0003677molecular_functionDNA binding
d0005515molecular_functionprotein binding
d0005634cellular_componentnucleus
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
e0030527molecular_functionstructural constituent of chromatin
e0046982molecular_functionprotein heterodimerization activity
f0000786cellular_componentnucleosome
f0003677molecular_functionDNA binding
f0005515molecular_functionprotein binding
f0005634cellular_componentnucleus
f0005694cellular_componentchromosome
f0006334biological_processnucleosome assembly
f0030527molecular_functionstructural constituent of chromatin
f0046982molecular_functionprotein heterodimerization activity
g0000786cellular_componentnucleosome
g0003677molecular_functionDNA binding
g0005634cellular_componentnucleus
g0005694cellular_componentchromosome
g0030527molecular_functionstructural constituent of chromatin
g0031507biological_processheterochromatin formation
g0046982molecular_functionprotein heterodimerization activity
h0000786cellular_componentnucleosome
h0003677molecular_functionDNA binding
h0005515molecular_functionprotein binding
h0005634cellular_componentnucleus
h0005694cellular_componentchromosome
h0030527molecular_functionstructural constituent of chromatin
h0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
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

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

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4
ChainResidueDetails
DSER3
dGLY10
dLYS13
dTHR18
hSER3
hGLY10
hLYS13
hTHR18
DGLY10
DLYS13
DTHR18
HSER3
HGLY10
HLYS13
HTHR18
dSER3

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12757711
ChainResidueDetails
DLYS12
HLYS12
dLYS12
hLYS12

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DGLU110
HGLU110
dGLU110
hGLU110
cTHR10
cLEU96
gTHR10
gLEU96

site_idSWS_FT_FI4
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4
ChainResidueDetails
DTYR118
GGLY37
HTYR118
gGLY37
dTYR118
hTYR118

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS75
bARG17
bARG45
bTHR80
fGLY9
fARG17
fARG45
fTHR80
CTHR76
GLYS75
GTHR76
cLYS75
cTHR76
gLYS75
gTHR76
bGLY9

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N5-methylglutamine => ECO:0000250
ChainResidueDetails
CGLY105
GGLY105
cGLY105
gGLY105
bGLY13
bVAL21
fGLY13
fVAL21

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS119
GLYS119
cLYS119
gLYS119
bPRO32
bARG92
fPRO32
fARG92

site_idSWS_FT_FI8
Number of Residues16
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
ChainResidueDetails
CALA14
cTHR16
cTHR120
gALA14
gTHR16
gTHR120
FGLY48
CTHR16
CTHR120
GALA14
GTHR16
GTHR120
cALA14

site_idSWS_FT_FI9
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BGLU52
BALA89
FGLU52
FALA89
bGLU52
bALA89
fGLU52
fALA89

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BVAL60
ELEU65
aGLN19
aALA24
aSER28
aLYS37
aLEU65
eGLN19
eALA24
eSER28
eLYS37
FVAL60
eLEU65
bVAL60
fVAL60
ALEU65
EGLN19
EALA24
ESER28
ELYS37

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BARG78
FARG78
bARG78
fARG78

site_idSWS_FT_FI12
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BPRO32
FPRO32
bPRO32
fPRO32

site_idSWS_FT_FI13
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
APRO38
BARG92
aPRO38
FARG92
bARG92
fARG92

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AARG42
EARG42
aARG42
eARG42

site_idSWS_FT_FI15
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ASER57
ATHR80
ESER57
ETHR80
aSER57
aTHR80
eSER57
eTHR80

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR58
ETHR58
aTHR58
eTHR58

site_idSWS_FT_FI17
Number of Residues8
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AASP81
AASN108
EASP81
EASN108
aASP81
aASN108
eASP81
eASN108

site_idSWS_FT_FI18
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER87
ESER87
aSER87
eSER87

site_idSWS_FT_FI19
Number of Residues4
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AARG116
EARG116
aARG116
eARG116

site_idSWS_FT_FI20
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AASP123
EASP123
aASP123
eASP123

site_idSWS_FT_FI21
Number of Residues4
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AALA111
EALA111
aALA111
eALA111

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon