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 | 20 |
Details | binding site for residue ADP A 301 |
Chain | Residue |
A | ASN40 |
A | PHE128 |
A | THR174 |
A | MG302 |
A | HOH429 |
A | HOH430 |
A | HOH431 |
A | HOH432 |
A | HOH434 |
A | HOH435 |
A | HOH468 |
A | ALA44 |
A | HOH475 |
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 | ADP301 |
A | HOH429 |
A | HOH430 |
A | HOH431 |
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 | |