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 |
| 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 |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006457 | biological_process | protein folding |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| G | 0051082 | molecular_function | unfolded protein binding |
| G | 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 9J0 A 301 |
| Chain | Residue |
| A | PHE22 |
| A | TYR139 |
| A | TRP162 |
| A | PHE170 |
| A | THR184 |
| A | HOH412 |
| A | HOH429 |
| A | ALA55 |
| A | ASP93 |
| A | MET98 |
| A | LEU103 |
| A | ILE104 |
| A | GLY108 |
| A | GLY135 |
| A | PHE138 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 9J0 C 301 |
| Chain | Residue |
| C | SER52 |
| C | ALA55 |
| C | ASP93 |
| C | MET98 |
| C | LEU103 |
| C | ILE104 |
| C | GLY108 |
| C | GLY135 |
| C | PHE138 |
| C | TYR139 |
| C | TRP162 |
| C | PHE170 |
| C | HOH404 |
| C | HOH411 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue 9J0 E 301 |
| Chain | Residue |
| E | PHE22 |
| E | SER52 |
| E | ALA55 |
| E | ASP93 |
| E | MET98 |
| E | LEU103 |
| E | ILE104 |
| E | GLY108 |
| E | GLY135 |
| E | PHE138 |
| E | TYR139 |
| E | TRP162 |
| E | PHE170 |
| E | HOH401 |
| E | HOH406 |
| E | HOH411 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue 9J0 G 301 |
| Chain | Residue |
| G | PHE22 |
| G | SER52 |
| G | ALA55 |
| G | ASP93 |
| G | MET98 |
| G | LEU103 |
| G | ILE104 |
| G | GLY108 |
| G | PHE138 |
| G | TYR139 |
| G | TRP162 |
| G | PHE170 |
| G | THR184 |
| G | HOH406 |
| G | HOH422 |
| G | HOH423 |
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 | TYR38-GLU47 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]} |
