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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue RDC A 301 |
Chain | Residue |
A | ASN40 |
A | PHE127 |
A | THR174 |
A | LEU176 |
A | HOH414 |
A | HOH473 |
A | ASP43 |
A | ALA44 |
A | LYS47 |
A | ASP82 |
A | ILE85 |
A | MET87 |
A | ASN95 |
A | LEU96 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue RDC B 301 |
Chain | Residue |
B | ASN40 |
B | ASP43 |
B | ALA44 |
B | LYS47 |
B | ASP82 |
B | MET87 |
B | LEU96 |
B | PHE127 |
B | THR174 |
B | LEU176 |
B | HOH414 |
B | HOH460 |
B | HOH486 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG B 302 |
Chain | Residue |
B | SER42 |
B | VAL204 |
B | ALA205 |
B | HOH439 |
B | HOH480 |
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 | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | LYS101 | |
B | PHE127 | |
A | ASN40 | |
A | ASP82 | |
A | LYS101 | |
A | PHE127 | |
B | ASN40 | |
B | ASP82 | |