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8VO0

H3K36me3-modified nucleosome bound to PRC2_AJ1-450 with histone H3 tail disengaged

Functional Information from GO Data
ChainGOidnamespacecontents
I0000786cellular_componentnucleosome
I0003677molecular_functionDNA binding
I0030527molecular_functionstructural constituent of chromatin
I0046982molecular_functionprotein heterodimerization activity
J0003677molecular_functionDNA binding
J0030527molecular_functionstructural constituent of chromatin
J0046982molecular_functionprotein heterodimerization activity
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0030527molecular_functionstructural constituent of chromatin
K0046982molecular_functionprotein heterodimerization activity
M0000786cellular_componentnucleosome
M0003677molecular_functionDNA binding
M0030527molecular_functionstructural constituent of chromatin
M0046982molecular_functionprotein heterodimerization activity
O0000786cellular_componentnucleosome
O0003677molecular_functionDNA binding
O0030527molecular_functionstructural constituent of chromatin
O0046982molecular_functionprotein heterodimerization activity
Q0003677molecular_functionDNA binding
Q0030527molecular_functionstructural constituent of chromatin
Q0046982molecular_functionprotein heterodimerization activity
R0000786cellular_componentnucleosome
R0003677molecular_functionDNA binding
R0030527molecular_functionstructural constituent of chromatin
R0046982molecular_functionprotein heterodimerization activity
S0000786cellular_componentnucleosome
S0003677molecular_functionDNA binding
S0030527molecular_functionstructural constituent of chromatin
S0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
KALA21-VAL27

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
MARG89-GLY111
SARG89-GLY111

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
IPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980
ChainResidueDetails
ITYR41
OTYR41
JLYS91

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
ILYS56
OLYS56

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ISER57
OSER57

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708
ChainResidueDetails
ILYS64
OLYS64

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
ILYS79
OLYS79

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ITHR80
OTHR80

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ISER86
OSER86

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ITHR107
OTHR107

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ILYS115
OLYS115

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ILYS122
OLYS122

site_idSWS_FT_FI11
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21076176
ChainResidueDetails
ICYS110
OCYS110

237423

PDB entries from 2025-06-11

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