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 | 19 |
| Details | binding site for residue GDM A 301 |
| Chain | Residue |
| A | ASN40 |
| A | ARG101 |
| A | GLY125 |
| A | VAL126 |
| A | GLY127 |
| A | PHE128 |
| A | THR174 |
| A | HOH450 |
| A | HOH456 |
| A | HOH467 |
| A | HOH503 |
| A | ALA41 |
| A | ASP43 |
| A | ALA44 |
| A | LYS47 |
| A | ASP82 |
| A | ILE85 |
| A | MET87 |
| A | ASN95 |
Functional Information from PROSITE/UniProt
| site_id | PS00298 |
| Number of Residues | 10 |
| Details | HSP90 Heat shock hsp90 proteins family signature. YsNKEVFLRE |
| Chain | Residue | Details |
| A | TYR27-GLU36 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN40 | |
| A | ASP82 | |
| A | ASN95 | |
| A | PHE128 | |
