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 | 18 |
Details | binding site for residue 2GJ A 301 |
Chain | Residue |
A | ASN40 |
A | ASN95 |
A | PHE123 |
A | GLY124 |
A | THR174 |
A | LEU176 |
A | HOH411 |
A | HOH423 |
A | HOH468 |
A | HOH488 |
A | ALA44 |
A | LYS47 |
A | TYR50 |
A | ASP82 |
A | ILE85 |
A | GLY86 |
A | MET87 |
A | ASP91 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | GLN122 |
A | LYS199 |
A | HOH426 |
A | HOH542 |
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 | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | PHE127 | |
A | ASN40 | |
A | ASP82 | |
A | LYS101 | |