6IQ4
Nucleosome core particle cross-linked with a hetero-binuclear molecule possessing RAPTA and gold(I) 4-(diphenylphosphino)benzoic acid groups.
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 | 2 |
| Details | binding site for residue AU A 201 |
| Chain | Residue |
| A | HIS113 |
| A | XIS202 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue XIS A 202 |
| Chain | Residue |
| A | ILE112 |
| A | AU201 |
| A | HOH302 |
| E | LYS122 |
| E | GLN125 |
| E | ARG129 |
| E | ARG134 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 201 |
| Chain | Residue |
| D | VAL45 |
| D | HOH301 |
| E | ASP77 |
| E | HOH312 |
| E | HOH317 |
| F | HOH204 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue D0X G 201 |
| Chain | Residue |
| G | TYR57 |
| G | GLU61 |
| G | GLU64 |
| H | HIS106 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue MG I 101 |
| Chain | Residue |
| I | DG60 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue MG I 102 |
| Chain | Residue |
| I | DA3 |
| I | HOH202 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue MG J 101 |
| Chain | Residue |
| J | DG60 |
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 | 4 |
| Details | DNA_BIND: |
| Chain | Residue | Details |
| F | LYS16-LYS20 | |
| D | LYS113 | |
| D | LYS117 | |
| H | LYS31 | |
| H | LYS113 | |
| H | LYS117 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393 |
| Chain | Residue | Details |
| F | LYS16 | |
| F | LYS44 | |
| G | LYS74 | |
| G | LYS75 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793 |
| Chain | Residue | Details |
| F | LYS20 | |
| H | SER33 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
| Chain | Residue | Details |
| F | LYS31 | |
| F | LYS77 | |
| F | LYS91 | |
| H | LYS82 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| F | SER47 | |
| D | LYS105 | |
| H | LYS43 | |
| H | LYS105 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| F | TYR51 | |
| H | LYS54 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
| Chain | Residue | Details |
| F | LYS59 | |
| H | ARG76 | |
| G | LYS119 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| F | LYS79 | |
| D | ARG89 | |
| H | ARG83 | |
| H | ARG89 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| F | THR80 | |
| H | THR112 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| F | TYR88 | |
| H | SER109 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| F | LYS20 | |
| F | LYS59 | |
| F | LYS79 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714 |
| Chain | Residue | Details |
| F | LYS91 | |
| H | LYS117 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146 |
| Chain | Residue | Details |
| F | LYS31 |
