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 | 14 |
| Details | binding site for residue RDC A 301 |
| Chain | Residue |
| A | ASN40 |
| A | PHE127 |
| A | THR174 |
| A | LEU176 |
| A | HOH414 |
| A | HOH473 |
| A | ASP43 |
| A | ALA44 |
| A | LYS47 |
| A | ASP82 |
| A | ILE85 |
| A | MET87 |
| A | ASN95 |
| A | LEU96 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue RDC B 301 |
| Chain | Residue |
| B | ASN40 |
| B | ASP43 |
| B | ALA44 |
| B | LYS47 |
| B | ASP82 |
| B | MET87 |
| B | LEU96 |
| B | PHE127 |
| B | THR174 |
| B | LEU176 |
| B | HOH414 |
| B | HOH460 |
| B | HOH486 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | SER42 |
| B | VAL204 |
| B | ALA205 |
| B | HOH439 |
| B | HOH480 |
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 | TYR27-GLU36 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
