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 | 16 |
Details | binding site for residue N5O A 301 |
Chain | Residue |
A | ASN51 |
A | THR184 |
A | HOH401 |
A | HOH424 |
A | HOH479 |
A | HOH559 |
A | HOH572 |
A | HOH603 |
A | ALA55 |
A | ASP93 |
A | MET98 |
A | ASN106 |
A | SER113 |
A | GLY135 |
A | VAL136 |
A | TYR139 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MG A 302 |
Chain | Residue |
A | GLU62 |
A | LYS69 |
A | ILE96 |
A | ASN155 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue MG B 301 |
Chain | Residue |
B | ILE110 |
B | SER113 |
B | HOH602 |
B | HOH691 |
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 | 6 |
Details | Binding site: {} |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]} |