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 |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BC2 A 1001 |
| Chain | Residue |
| A | ASP109 |
| A | PHE194 |
| A | THR241 |
| A | ALA110 |
| A | ASP148 |
| A | ASP157 |
| A | ASN161 |
| A | ILE165 |
| A | GLY191 |
| A | VAL192 |
| A | GLY193 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BC2 B 1001 |
| Chain | Residue |
| B | ASP109 |
| B | ALA110 |
| B | ASP148 |
| B | ASP157 |
| B | ASN161 |
| B | ILE165 |
| B | GLY191 |
| B | VAL192 |
| B | GLY193 |
| B | PHE194 |
| B | THR241 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | ARG134 |
| A | THR147 |
| A | ARG242 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2 |
| Chain | Residue |
| B | ARG134 |
| B | THR147 |
| B | ARG242 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3 |
| Chain | Residue |
| B | ALA137 |
| B | LYS139 |
| B | GLU140 |
| B | LYS324 |
Functional Information from PROSITE/UniProt
| site_id | PS00298 |
| Number of Residues | 10 |
| Details | HSP90 Heat shock hsp90 proteins family signature. YtQKEVFLRE |
| Chain | Residue | Details |
| A | TYR93-GLU102 | |
