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8Q3X

Structure of Nucleosome Core with a Bound Metallopeptide Conjugate (Kaposi Sarcoma Associated Herpesvirus LANA Peptide-Au[I] Compound)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000786cellular_componentnucleosome
AAA0003677molecular_functionDNA binding
AAA0030527molecular_functionstructural constituent of chromatin
AAA0046982molecular_functionprotein heterodimerization activity
BBB0003677molecular_functionDNA binding
BBB0030527molecular_functionstructural constituent of chromatin
BBB0046982molecular_functionprotein heterodimerization activity
CCC0000786cellular_componentnucleosome
CCC0003677molecular_functionDNA binding
CCC0030527molecular_functionstructural constituent of chromatin
CCC0046982molecular_functionprotein heterodimerization activity
DDD0000786cellular_componentnucleosome
DDD0003677molecular_functionDNA binding
DDD0030527molecular_functionstructural constituent of chromatin
DDD0046982molecular_functionprotein heterodimerization activity
EEE0000786cellular_componentnucleosome
EEE0003677molecular_functionDNA binding
EEE0030527molecular_functionstructural constituent of chromatin
EEE0046982molecular_functionprotein heterodimerization activity
FFF0003677molecular_functionDNA binding
FFF0030527molecular_functionstructural constituent of chromatin
FFF0046982molecular_functionprotein heterodimerization activity
GGG0000786cellular_componentnucleosome
GGG0003677molecular_functionDNA binding
GGG0030527molecular_functionstructural constituent of chromatin
GGG0046982molecular_functionprotein heterodimerization activity
HHH0000786cellular_componentnucleosome
HHH0003677molecular_functionDNA binding
HHH0030527molecular_functionstructural constituent of chromatin
HHH0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CCCALA21-VAL27

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DDDARG89-GLY111

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
AAAPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
DDDLYS31
DDDLYS113
DDDLYS117
HHHLYS31
HHHLYS113
HHHLYS117

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
DDDGLU32
HHHGLU32
FFFLYS16
FFFLYS44

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q8CGP1
ChainResidueDetails
DDDSER33
HHHSER33
GGGLYS74
GGGLYS75

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
DDDLYS40
DDDLYS82
HHHLYS40
HHHLYS82
FFFLYS77
FFFLYS91

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
DDDLYS43
DDDLYS105
HHHLYS43
HHHLYS105

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
DDDLYS54
HHHLYS54
GGGLYS118
GGGLYS119

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DDDARG76
HHHARG76

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DDDARG83
DDDARG89
HHHARG83
HHHARG89

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DDDTHR112
HHHTHR112

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DDDSER109
HHHSER109

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
DDDLYS31
HHHLYS31
BBBLYS79
FFFLYS20
FFFLYS59
FFFLYS79

site_idSWS_FT_FI12
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
DDDLYS117
HHHLYS117

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
BBBLYS31
FFFLYS31

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PDB entries from 2024-10-30

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