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 | 14 |
| Details | binding site for residue FEU A 301 |
| Chain | Residue |
| A | ALA123 |
| A | TRP231 |
| A | THR251 |
| A | HOH449 |
| A | HOH504 |
| A | HOH516 |
| A | ASP158 |
| A | ILE161 |
| A | GLY162 |
| A | MET163 |
| A | GLU167 |
| A | LEU168 |
| A | LEU172 |
| A | PHE205 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN119 | |
| A | ASP158 | |
| A | ASN171 | |
| A | PHE205 | |
| Chain | Residue | Details |
| A | SER170 | |
| Chain | Residue | Details |
| A | THR174 | |
| Chain | Residue | Details |
| A | SER194 | |
| Chain | Residue | Details |
| A | LYS262 | |
