6LE9
The Human Telomeric Nucleosome Displays Distinct Structural and Dynamic Properties
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000786 | cellular_component | nucleosome |
| A | 0003677 | molecular_function | DNA binding |
| A | 0030527 | molecular_function | structural constituent of chromatin |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0003677 | molecular_function | DNA binding |
| B | 0030527 | molecular_function | structural constituent of chromatin |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0000786 | cellular_component | nucleosome |
| C | 0003677 | molecular_function | DNA binding |
| C | 0030527 | molecular_function | structural constituent of chromatin |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0000786 | cellular_component | nucleosome |
| D | 0003677 | molecular_function | DNA binding |
| D | 0030527 | molecular_function | structural constituent of chromatin |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| E | 0000786 | cellular_component | nucleosome |
| E | 0003677 | molecular_function | DNA binding |
| E | 0030527 | molecular_function | structural constituent of chromatin |
| E | 0046982 | molecular_function | protein heterodimerization activity |
| F | 0003677 | molecular_function | DNA binding |
| F | 0030527 | molecular_function | structural constituent of chromatin |
| F | 0046982 | molecular_function | protein heterodimerization activity |
| G | 0000786 | cellular_component | nucleosome |
| G | 0003677 | molecular_function | DNA binding |
| G | 0030527 | molecular_function | structural constituent of chromatin |
| G | 0046982 | molecular_function | protein heterodimerization activity |
| H | 0000786 | cellular_component | nucleosome |
| H | 0003677 | molecular_function | DNA binding |
| H | 0030527 | molecular_function | structural constituent of chromatin |
| H | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue MN A 201 |
| Chain | Residue |
| A | GLN76 |
| A | ASP77 |
| H | VAL45 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue MN I 101 |
| Chain | Residue |
| I | DA38 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue MN J 101 |
| Chain | Residue |
| I | DA-27 |
| J | DG26 |
| J | DT27 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue MN J 102 |
| Chain | Residue |
| J | DG6 |
| J | DG7 |
Functional Information from PROSITE/UniProt
| site_id | PS00046 |
| Number of Residues | 7 |
| Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
| Chain | Residue | Details |
| C | ALA21-VAL27 |
| site_id | PS00357 |
| Number of Residues | 23 |
| Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
| Chain | Residue | Details |
| D | ARG89-GLY111 |
| site_id | PS00959 |
| Number of Residues | 9 |
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
| Chain | Residue | Details |
| A | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
| Chain | Residue | Details |
| D | LYS31 | |
| D | LYS113 | |
| D | LYS117 | |
| H | LYS31 | |
| H | LYS113 | |
| H | LYS117 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 |
| Chain | Residue | Details |
| D | GLU32 | |
| H | GLU32 | |
| G | LYS74 | |
| G | LYS75 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q8CGP1 |
| Chain | Residue | Details |
| D | SER33 | |
| H | SER33 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 |
| Chain | Residue | Details |
| D | LYS40 | |
| D | LYS82 | |
| H | LYS40 | |
| H | LYS82 | |
| F | LYS77 | |
| F | LYS91 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 |
| Chain | Residue | Details |
| D | LYS43 | |
| D | LYS105 | |
| H | LYS43 | |
| H | LYS105 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 |
| Chain | Residue | Details |
| D | LYS54 | |
| H | LYS54 | |
| G | LYS15 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 |
| Chain | Residue | Details |
| D | ARG76 | |
| H | ARG76 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 |
| Chain | Residue | Details |
| D | ARG83 | |
| D | ARG89 | |
| H | ARG83 | |
| H | ARG89 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729 |
| Chain | Residue | Details |
| D | THR112 | |
| H | THR112 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 |
| Chain | Residue | Details |
| D | SER109 | |
| H | SER109 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 |
| Chain | Residue | Details |
| D | LYS31 | |
| H | LYS31 | |
| B | LYS79 | |
| F | LYS20 | |
| F | LYS59 | |
| F | LYS79 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563 |
| Chain | Residue | Details |
| D | LYS117 | |
| H | LYS117 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146 |
| Chain | Residue | Details |
| B | LYS31 | |
| F | LYS31 |
