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6PA7

The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome.

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
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
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
K0006306biological_processobsolete DNA methylation
K0008168molecular_functionmethyltransferase activity
K0010468biological_processregulation of gene expression
N0000122biological_processnegative regulation of transcription by RNA polymerase II
N0003677molecular_functionDNA binding
N0003714molecular_functiontranscription corepressor activity
N0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0006306biological_processobsolete DNA methylation
N0008168molecular_functionmethyltransferase activity
N0009008molecular_functionDNA-methyltransferase activity
N0010468biological_processregulation of gene expression
N0010605biological_processnegative regulation of macromolecule metabolic process
N0010628biological_processpositive regulation of gene expression
N0016740molecular_functiontransferase activity
N0032259biological_processmethylation
N0032776biological_processobsolete DNA methylation on cytosine
N0046872molecular_functionmetal ion binding
N0051718molecular_functionDNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates
N1902494cellular_componentcatalytic complex
P0006306biological_processobsolete DNA methylation
P0008168molecular_functionmethyltransferase activity
P0010468biological_processregulation of gene expression
S0000122biological_processnegative regulation of transcription by RNA polymerase II
S0003677molecular_functionDNA binding
S0003714molecular_functiontranscription corepressor activity
S0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
S0005515molecular_functionprotein binding
S0005634cellular_componentnucleus
S0005654cellular_componentnucleoplasm
S0006306biological_processobsolete DNA methylation
S0008168molecular_functionmethyltransferase activity
S0009008molecular_functionDNA-methyltransferase activity
S0010468biological_processregulation of gene expression
S0010605biological_processnegative regulation of macromolecule metabolic process
S0010628biological_processpositive regulation of gene expression
S0016740molecular_functiontransferase activity
S0032259biological_processmethylation
S0032776biological_processobsolete DNA methylation on cytosine
S0046872molecular_functionmetal ion binding
S0051718molecular_functionDNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates
S1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 201
ChainResidue
APRO121
ALYS122

site_idAC2
Number of Residues4
Detailsbinding site for residue CL C 201
ChainResidue
CGLY46
DTHR87
DSER88
IDT122

site_idAC3
Number of Residues3
Detailsbinding site for residue CL H 201
ChainResidue
GGLY46
HTHR87
HSER88

site_idAC4
Number of Residues14
Detailsbinding site for residue SAH K 1001
ChainResidue
KPHE640
KASP641
KSER663
KGLU664
KVAL665
KCYS666
KASP686
KVAL687
KGLY707
KLEU730
KGLU756
KARG891
KSER892
KTRP893

site_idAC5
Number of Residues14
Detailsbinding site for residue SAH P 1001
ChainResidue
PPHE640
PASP641
PSER663
PGLU664
PVAL665
PCYS666
PASP686
PVAL687
PGLY707
PLEU730
PGLU756
PARG891
PSER892
PTRP893

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

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

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

site_idPS00094
Number of Residues13
DetailsC5_MTASE_1 C-5 cytosine-specific DNA methylases active site. DlVigGsPCnDLS
ChainResidueDetails
NASP623-SER635
KASP702-SER714

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

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 Residues60
DetailsZN_FING: GATA-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00865
ChainResidueDetails
NLEU434-GLY464
SLEU434-GLY464
DLYS12
DLYS17
HLYS2
HLYS9
HLYS12
HLYS17

site_idSWS_FT_FI2
Number of Residues112
DetailsZN_FING: PHD-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00865
ChainResidueDetails
NCYS475-THR531
SCYS475-THR531

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01016, ECO:0000255|PROSITE-ProRule:PRU10018
ChainResidueDetails
NLEU651
SLEU651
GLYS9
GLYS95

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y6K1
ChainResidueDetails
NVAL582
NVAL605
NGLY627
SVAL582
SVAL605
SGLY627
PASP686
PARG891

site_idSWS_FT_FI5
Number of Residues10
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
NSER82
SSER202
NSER100
NSER110
NSER195
NSER202
SSER82
SSER100
SSER110
SSER195

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:21406692
ChainResidueDetails
NTHR96
STHR96
PSER255
PSER267

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
NSER136
SSER136
FLYS31
FLYS91

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
NSER209
SSER209
PSER390
PSER393
GLYS13
GLYS15
GLYS119

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Citrulline => ECO:0000250
ChainResidueDetails
NSER410
SSER410
FTYR51
FTYR88

site_idSWS_FT_FI10
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
NLYS89
ELYS64
FLYS59
NGLU617
SLYS89
ALYS64
SGLU617
ELYS23
ELYS27
ELYS36

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BLYS77
FLYS77

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BLYS31
FLYS31

site_idSWS_FT_FI13
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
ALYS37
BLYS91
FLYS91

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATYR41
ETYR41

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ALYS56
ALYS79
ELYS56
ELYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ASER57
ESER57

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR80
ATHR107
ETHR80
ETHR107

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI21
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ACYS110
ECYS110

218853

PDB entries from 2024-04-24

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