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3AZE

Crystal Structure of Human Nucleosome Core Particle Containing H3K64Q mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0010467biological_processgene expression
A0016020cellular_componentmembrane
A0030527molecular_functionstructural constituent of chromatin
A0032200biological_processtelomere organization
A0032991cellular_componentprotein-containing complex
A0040029biological_processepigenetic regulation of gene expression
A0045296molecular_functioncadherin binding
A0046982molecular_functionprotein heterodimerization activity
A0070062cellular_componentextracellular exosome
B0000781cellular_componentchromosome, telomeric region
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0016020cellular_componentmembrane
B0030527molecular_functionstructural constituent of chromatin
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0043505cellular_componentCENP-A containing nucleosome
B0045653biological_processnegative regulation of megakaryocyte differentiation
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
B0070062cellular_componentextracellular exosome
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006325biological_processchromatin organization
C0008285biological_processnegative regulation of cell population proliferation
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
C0043505cellular_componentCENP-A containing nucleosome
C0046982molecular_functionprotein heterodimerization activity
C0061644biological_processprotein localization to CENP-A containing chromatin
C0070062cellular_componentextracellular exosome
D0000786cellular_componentnucleosome
D0001530molecular_functionlipopolysaccharide binding
D0002227biological_processinnate immune response in mucosa
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006325biological_processchromatin organization
D0006334biological_processnucleosome assembly
D0010804biological_processnegative regulation of tumor necrosis factor-mediated signaling pathway
D0019731biological_processantibacterial humoral response
D0030527molecular_functionstructural constituent of chromatin
D0031640biological_processkilling of cells of another organism
D0042742biological_processdefense response to bacterium
D0043505cellular_componentCENP-A containing nucleosome
D0046982molecular_functionprotein heterodimerization activity
D0050829biological_processdefense response to Gram-negative bacterium
D0050830biological_processdefense response to Gram-positive bacterium
D0061644biological_processprotein localization to CENP-A containing chromatin
D0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0010467biological_processgene expression
E0016020cellular_componentmembrane
E0030527molecular_functionstructural constituent of chromatin
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0040029biological_processepigenetic regulation of gene expression
E0045296molecular_functioncadherin binding
E0046982molecular_functionprotein heterodimerization activity
E0070062cellular_componentextracellular exosome
F0000781cellular_componentchromosome, telomeric region
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0003723molecular_functionRNA binding
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0016020cellular_componentmembrane
F0030527molecular_functionstructural constituent of chromatin
F0032200biological_processtelomere organization
F0032991cellular_componentprotein-containing complex
F0043505cellular_componentCENP-A containing nucleosome
F0045653biological_processnegative regulation of megakaryocyte differentiation
F0046982molecular_functionprotein heterodimerization activity
F0061644biological_processprotein localization to CENP-A containing chromatin
F0070062cellular_componentextracellular exosome
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0006325biological_processchromatin organization
G0008285biological_processnegative regulation of cell population proliferation
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0043505cellular_componentCENP-A containing nucleosome
G0046982molecular_functionprotein heterodimerization activity
G0061644biological_processprotein localization to CENP-A containing chromatin
G0070062cellular_componentextracellular exosome
H0000786cellular_componentnucleosome
H0001530molecular_functionlipopolysaccharide binding
H0002227biological_processinnate immune response in mucosa
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005615cellular_componentextracellular space
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0005829cellular_componentcytosol
H0005886cellular_componentplasma membrane
H0006325biological_processchromatin organization
H0006334biological_processnucleosome assembly
H0010804biological_processnegative regulation of tumor necrosis factor-mediated signaling pathway
H0019731biological_processantibacterial humoral response
H0030527molecular_functionstructural constituent of chromatin
H0031640biological_processkilling of cells of another organism
H0042742biological_processdefense response to bacterium
H0043505cellular_componentCENP-A containing nucleosome
H0046982molecular_functionprotein heterodimerization activity
H0050829biological_processdefense response to Gram-negative bacterium
H0050830biological_processdefense response to Gram-positive bacterium
H0061644biological_processprotein localization to CENP-A containing chromatin
H0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1001
ChainResidue
APRO121
ALYS122

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN D 201
ChainResidue
DVAL48
EASP77

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL D 202
ChainResidue
CALA45
CGLY46
DTHR90
DSER91

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL E 1001
ChainResidue
ELYS122
EPRO121

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL G 1001
ChainResidue
GGLY44
GALA45
GGLY46
HTHR90
HSER91

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN I 1001
ChainResidue
IDG68

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN I 1002
ChainResidue
IDT120
IDG121

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN I 1003
ChainResidue
IDC132
IDA133
IDG134

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN I 1004
ChainResidue
IDA99
IDG100

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN I 1005
ChainResidue
IDC114

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN J 1001
ChainResidue
JDG185
JDG186

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 1002
ChainResidue
JDG267

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 1003
ChainResidue
JDG217

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MN J 1004
ChainResidue
JDG280

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
DARG92-GLY114

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 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:0000269|PubMed:27530147
ChainResidueDetails
DGLU2
HGLU2

site_idSWS_FT_FI3
Number of Residues16
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
DLYS5
HLYS11
HLYS15
HLYS16
HLYS20
HLYS23
HLYS43
HLYS85
DLYS11
DLYS15
DLYS16
DLYS20
DLYS23
DLYS43
DLYS85
HLYS5

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:34874266
ChainResidueDetails
DSER6
HSER6
GLYS9
GLYS95

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:12757711
ChainResidueDetails
DSER14
HSER14
BLYS77
BLYS91
FLYS12
FLYS31
FLYS77
FLYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS24
HLYS24
GLYS74
GLYS75

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
DLYS34
DLYS116
DLYS120
HLYS34
HLYS116
HLYS120

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
DGLU35
HGLU35
CLYS125
GLYS118
GLYS119
GLYS125

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
DSER36
HSER36
ELYS14
ELYS56

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
DLYS46
DLYS108
HLYS46
HLYS108

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS57
HLYS57
ELYS18
GLYS119

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG79
HARG79

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG86
DARG92
HARG86
HARG92

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DTHR115
HTHR115
FLYS91

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DSER112
HSER112
BLYS79
FLYS20
FLYS59
FLYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876
ChainResidueDetails
DLYS5
HLYS5

site_idSWS_FT_FI18
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563
ChainResidueDetails
ALYS37
DLYS120
HLYS120

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 Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
DLYS34
HLYS34

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
ALYS79
ELYS79

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ATHR80
ETHR80

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR107
ETHR107

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI27
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ALYS18
ELYS18

227111

PDB entries from 2024-11-06

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