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 | 13 |
Details | binding site for residue ACP A 301 |
Chain | Residue |
A | ASN39 |
A | THR173 |
A | HOH406 |
A | HOH417 |
A | HOH419 |
A | ALA43 |
A | ASP81 |
A | MET86 |
A | ASN94 |
A | LEU95 |
A | ARG100 |
A | GLY125 |
A | PHE126 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue PG4 A 302 |
Chain | Residue |
A | SER78 |
A | GLU167 |
A | LYS174 |
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 | TYR26-GLU35 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU35 | |
A | MET86 | |
A | ASN94 | |
A | SER101 | |
A | GLN121 | |
A | THR173 | |
Chain | Residue | Details |
A | ASN39 | |
A | ASP81 | |
A | PHE126 | |