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 |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 6TN B 301 |
| Chain | Residue |
| B | ASN51 |
| B | THR184 |
| B | VAL186 |
| B | HOH405 |
| B | HOH444 |
| B | HOH457 |
| D | TYR61 |
| B | ALA55 |
| B | LYS58 |
| B | ASP93 |
| B | ILE96 |
| B | GLY97 |
| B | MET98 |
| B | LEU107 |
| B | PHE138 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue 6TN A 301 |
| Chain | Residue |
| A | ASN51 |
| A | ALA55 |
| A | ASP93 |
| A | ILE96 |
| A | GLY97 |
| A | PHE138 |
| A | THR184 |
| A | VAL186 |
| A | HOH409 |
| A | HOH438 |
| C | TYR61 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue 6TN D 301 |
| Chain | Residue |
| B | TYR61 |
| D | ASN51 |
| D | ALA55 |
| D | ASP93 |
| D | ILE96 |
| D | GLY97 |
| D | PHE138 |
| D | THR184 |
| D | VAL186 |
| D | HOH421 |
| D | HOH452 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 6TN C 301 |
| Chain | Residue |
| A | TYR61 |
| C | ASN51 |
| C | ALA55 |
| C | LYS58 |
| C | ASP93 |
| C | ILE96 |
| C | GLY97 |
| C | MET98 |
| C | LEU107 |
| C | PHE138 |
| C | THR184 |
| C | VAL186 |
| C | HOH414 |
| C | HOH437 |
Functional Information from PROSITE/UniProt
| site_id | PS00298 |
| Number of Residues | 10 |
| Details | HSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE |
| Chain | Residue | Details |
| B | TYR38-GLU47 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ASN51 | |
| C | ASN51 | |
| C | ASP93 | |
| C | PHE138 | |
| B | ASP93 | |
| B | PHE138 | |
| A | ASN51 | |
| A | ASP93 | |
| A | PHE138 | |
| D | ASN51 | |
| D | ASP93 | |
| D | PHE138 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | LYS112 | |
| A | LYS112 | |
| D | LYS112 | |
| C | LYS112 | |
| Chain | Residue | Details |
| B | LYS58 | |
| B | LYS84 | |
| A | LYS58 | |
| A | LYS84 | |
| D | LYS58 | |
| D | LYS84 | |
| C | LYS58 | |
| C | LYS84 | |
