Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
P | 0000786 | cellular_component | nucleosome |
P | 0003677 | molecular_function | DNA binding |
P | 0030527 | molecular_function | structural constituent of chromatin |
P | 0046982 | molecular_function | protein heterodimerization activity |
Q | 0000786 | cellular_component | nucleosome |
Q | 0003677 | molecular_function | DNA binding |
Q | 0030527 | molecular_function | structural constituent of chromatin |
Q | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 501 |
Chain | Residue |
A | CYS413 |
A | CYS416 |
A | CYS435 |
A | CYS446 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for residue ANP A 502 |
Chain | Residue |
A | MET72 |
A | MET80 |
A | SER86 |
A | LYS88 |
A | GLY98 |
A | LEU99 |
A | TYR100 |
A | GLY101 |
A | ASN102 |
A | GLY103 |
A | PHE104 |
A | LYS105 |
A | THR194 |
A | LYS358 |
A | MG503 |
A | GLU35 |
A | ASN39 |
A | ASP44 |
A | VAL45 |
A | ASP67 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue MG A 503 |
Chain | Residue |
A | GLU35 |
A | ASN39 |
A | ANP502 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | CYS413 |
B | CYS416 |
B | CYS435 |
B | CYS446 |
site_id | AC5 |
Number of Residues | 19 |
Details | binding site for residue ANP B 502 |
Chain | Residue |
B | ASN39 |
B | ASP44 |
B | VAL45 |
B | ASP67 |
B | MET72 |
B | MET80 |
B | SER86 |
B | LYS88 |
B | GLY98 |
B | LEU99 |
B | TYR100 |
B | GLY101 |
B | ASN102 |
B | GLY103 |
B | PHE104 |
B | LYS105 |
B | THR194 |
B | LYS358 |
B | MG503 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MG B 503 |
Chain | Residue |
B | GLU35 |
B | ASN39 |
B | ANP502 |
Functional Information from PROSITE/UniProt
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
P | LYS14-LEU20 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoarginine; alternate => ECO:0000305 |
Chain | Residue | Details |
P | ARG2 | |
Q | ARG2 | |
Chain | Residue | Details |
P | THR3 | |
Q | THR3 | |
A | CYS435 | |
A | CYS446 | |
B | CYS413 | |
B | CYS416 | |
B | CYS435 | |
B | CYS446 | |
Chain | Residue | Details |
P | LYS4 | |
B | LYS293 | |
Q | LYS4 | |
A | LYS205 | |
A | LYS280 | |
A | LYS293 | |
B | LYS191 | |
B | LYS205 | |
B | LYS280 | |
Chain | Residue | Details |
P | GLN5 | |
Q | GLN5 | |
Chain | Residue | Details |
P | THR6 | |
Q | THR6 | |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000269|PubMed:15485929 |
Chain | Residue | Details |
P | ARG8 | |
Q | ARG8 | |
Chain | Residue | Details |
P | LYS9 | |
P | LYS27 | |
Q | LYS9 | |
Q | LYS27 | |
Chain | Residue | Details |
P | SER10 | |
Q | SER10 | |
Chain | Residue | Details |
P | THR11 | |
Q | THR11 | |
Chain | Residue | Details |
P | LYS14 | |
Q | LYS14 | |
Chain | Residue | Details |
P | ARG17 | |
Q | ARG17 | |
Chain | Residue | Details |
P | LYS18 | |
P | LYS23 | |
Q | LYS18 | |
Q | LYS23 | |
Chain | Residue | Details |
P | ARG26 | |
Q | ARG26 | |
Chain | Residue | Details |
P | SER28 | |
Q | SER28 | |
Chain | Residue | Details |
P | LYS18 | |
Q | LYS18 | |