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 | 22 |
| Details | binding site for residue Q2A A 301 |
| Chain | Residue |
| A | ASN51 |
| A | GLY135 |
| A | PHE138 |
| A | TYR139 |
| A | VAL150 |
| A | TRP162 |
| A | THR184 |
| A | HOH404 |
| A | HOH409 |
| A | HOH429 |
| A | HOH432 |
| A | ALA55 |
| A | HOH491 |
| A | HOH524 |
| A | HOH543 |
| A | TYR61 |
| A | ASP93 |
| A | MET98 |
| A | ASP102 |
| A | ASN106 |
| A | LEU107 |
| A | ILE110 |
Functional Information from PROSITE/UniProt
| site_id | PS00298 |
| Number of Residues | 10 |
| Details | HSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE |
| Chain | Residue | Details |
| A | TYR38-GLU47 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN51 | |
| A | ASP93 | |
| A | PHE138 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS112 | |
| Chain | Residue | Details |
| A | THR5 | |
| A | THR7 | |
| Chain | Residue | Details |
| A | ARG58 | |
| A | LYS84 | |
| Chain | Residue | Details |
| A | SER231 | |
