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 | 14 |
Details | binding site for residue 6GV A 301 |
Chain | Residue |
A | ASN51 |
A | VAL150 |
A | THR184 |
A | VAL186 |
A | HOH410 |
A | HOH417 |
A | ALA55 |
A | LYS58 |
A | ASP93 |
A | ILE96 |
A | GLY97 |
A | MET98 |
A | LEU107 |
A | PHE138 |
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 | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN51 | |
A | ASP93 | |
A | PHE138 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS112 | |
Chain | Residue | Details |
A | LYS58 | |
A | LYS84 | |
Chain | Residue | Details |
A | SER231 | |