Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006457 | biological_process | protein folding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0051082 | molecular_function | unfolded protein binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | binding site for residue 8M9 A 601 |
Chain | Residue |
A | ALA123 |
A | VAL217 |
A | TRP231 |
A | THR251 |
A | HOH701 |
A | HOH718 |
A | HOH726 |
A | ASP158 |
A | ILE161 |
A | GLY162 |
A | MET163 |
A | LEU168 |
A | PHE201 |
A | PHE205 |
A | TYR206 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASN119 | |
A | ASP158 | |
A | ASN171 | |
A | PHE205 | |
A | ARG402 | |
Chain | Residue | Details |
A | SER170 | |
Chain | Residue | Details |
A | THR174 | |
Chain | Residue | Details |
A | SER194 | |
Chain | Residue | Details |
A | LYS262 | |
A | LYS324 | |
A | LYS431 | |
Chain | Residue | Details |
A | LYS332 | |
A | LYS424 | |
A | LYS466 | |
Chain | Residue | Details |
A | THR494 | |