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 | 26 |
| Details | BINDING SITE FOR RESIDUE ADP A 214 |
| Chain | Residue |
| A | ASN36 |
| A | PHE123 |
| A | THR169 |
| A | MG215 |
| A | HOH220 |
| A | HOH223 |
| A | HOH225 |
| A | HOH230 |
| A | HOH234 |
| A | HOH280 |
| A | HOH289 |
| A | ALA40 |
| A | HOH290 |
| A | HOH293 |
| A | HOH295 |
| A | HOH327 |
| A | HOH356 |
| A | HOH357 |
| A | HOH358 |
| A | ASP78 |
| A | MET83 |
| A | ASN91 |
| A | LEU92 |
| A | ARG97 |
| A | VAL121 |
| A | GLY122 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 215 |
| Chain | Residue |
| A | ASN36 |
| A | ADP214 |
| A | HOH356 |
| A | HOH357 |
| A | HOH358 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 216 |
| Chain | Residue |
| A | SER144 |
| A | THR158 |
| A | SER159 |
| A | THR160 |
| A | SER163 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 217 |
| Chain | Residue |
| A | LEU61 |
| A | TYR201 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 218 |
| Chain | Residue |
| A | SER53 |
| A | VAL54 |
| A | GLY56 |
| A | HOH229 |
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 | TYR23-GLU32 | |
