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 | 25 |
Details | binding site for residue AGS A 301 |
Chain | Residue |
A | ASN40 |
A | PHE128 |
A | THR174 |
A | MG302 |
A | HOH501 |
A | HOH511 |
A | HOH516 |
A | HOH517 |
A | HOH525 |
A | HOH526 |
A | HOH551 |
A | ALA44 |
A | HOH561 |
A | HOH564 |
A | HOH569 |
A | HOH600 |
A | HOH608 |
A | HOH686 |
A | ASP82 |
A | MET87 |
A | ASN95 |
A | LEU96 |
A | GLY125 |
A | VAL126 |
A | GLY127 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 302 |
Chain | Residue |
A | ASN40 |
A | AGS301 |
A | HOH525 |
A | HOH526 |
A | HOH551 |
Functional Information from PROSITE/UniProt
site_id | PS00298 |
Number of Residues | 10 |
Details | HSP90 Heat shock hsp90 proteins family signature. YsNKEVFLRE |
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 | ASN40 | |
A | ASP82 | |
A | ASN95 | |
A | PHE128 | |