8QKT
Structure of a nucleosome composed of a palindromic 167-base pair blunt-ended DNA fragment
This is a non-PDB format compatible entry.
Functional Information from GO Data
Chain | GOid | namespace | contents |
AAA | 0000786 | cellular_component | nucleosome |
AAA | 0003677 | molecular_function | DNA binding |
AAA | 0030527 | molecular_function | structural constituent of chromatin |
AAA | 0046982 | molecular_function | protein heterodimerization activity |
BBB | 0003677 | molecular_function | DNA binding |
BBB | 0030527 | molecular_function | structural constituent of chromatin |
BBB | 0046982 | molecular_function | protein heterodimerization activity |
CCC | 0000786 | cellular_component | nucleosome |
CCC | 0003677 | molecular_function | DNA binding |
CCC | 0030527 | molecular_function | structural constituent of chromatin |
CCC | 0046982 | molecular_function | protein heterodimerization activity |
DDD | 0000786 | cellular_component | nucleosome |
DDD | 0003677 | molecular_function | DNA binding |
DDD | 0030527 | molecular_function | structural constituent of chromatin |
DDD | 0046982 | molecular_function | protein heterodimerization activity |
EEE | 0000786 | cellular_component | nucleosome |
EEE | 0003677 | molecular_function | DNA binding |
EEE | 0030527 | molecular_function | structural constituent of chromatin |
EEE | 0046982 | molecular_function | protein heterodimerization activity |
FFF | 0003677 | molecular_function | DNA binding |
FFF | 0030527 | molecular_function | structural constituent of chromatin |
FFF | 0046982 | molecular_function | protein heterodimerization activity |
GGG | 0000786 | cellular_component | nucleosome |
GGG | 0003677 | molecular_function | DNA binding |
GGG | 0030527 | molecular_function | structural constituent of chromatin |
GGG | 0046982 | molecular_function | protein heterodimerization activity |
HHH | 0000786 | cellular_component | nucleosome |
HHH | 0003677 | molecular_function | DNA binding |
HHH | 0030527 | molecular_function | structural constituent of chromatin |
HHH | 0046982 | molecular_function | protein heterodimerization activity |
KKK | 0000786 | cellular_component | nucleosome |
KKK | 0003677 | molecular_function | DNA binding |
KKK | 0030527 | molecular_function | structural constituent of chromatin |
KKK | 0046982 | molecular_function | protein heterodimerization activity |
LLL | 0003677 | molecular_function | DNA binding |
LLL | 0030527 | molecular_function | structural constituent of chromatin |
LLL | 0046982 | molecular_function | protein heterodimerization activity |
MMM | 0000786 | cellular_component | nucleosome |
MMM | 0003677 | molecular_function | DNA binding |
MMM | 0030527 | molecular_function | structural constituent of chromatin |
MMM | 0046982 | molecular_function | protein heterodimerization activity |
NNN | 0000786 | cellular_component | nucleosome |
NNN | 0003677 | molecular_function | DNA binding |
NNN | 0030527 | molecular_function | structural constituent of chromatin |
NNN | 0046982 | molecular_function | protein heterodimerization activity |
OOO | 0000786 | cellular_component | nucleosome |
OOO | 0003677 | molecular_function | DNA binding |
OOO | 0030527 | molecular_function | structural constituent of chromatin |
OOO | 0046982 | molecular_function | protein heterodimerization activity |
PPP | 0003677 | molecular_function | DNA binding |
PPP | 0030527 | molecular_function | structural constituent of chromatin |
PPP | 0046982 | molecular_function | protein heterodimerization activity |
QQQ | 0000786 | cellular_component | nucleosome |
QQQ | 0003677 | molecular_function | DNA binding |
QQQ | 0030527 | molecular_function | structural constituent of chromatin |
QQQ | 0046982 | molecular_function | protein heterodimerization activity |
RRR | 0000786 | cellular_component | nucleosome |
RRR | 0003677 | molecular_function | DNA binding |
RRR | 0030527 | molecular_function | structural constituent of chromatin |
RRR | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
CCC | ALA21-VAL27 | |
GGG | ALA21-VAL27 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
DDD | ARG89-GLY111 | |
HHH | ARG89-GLY111 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
AAA | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19783980","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29211711","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"PubMed","id":"31542297","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27436229","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | Modified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q00729","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 4 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"21726816","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI22 |
Number of Residues | 8 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"16307923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713563","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |