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 | 8 |
Details | binding site for residue EDO A 301 |
Chain | Residue |
A | ASN40 |
A | ALA44 |
A | ASP82 |
A | THR174 |
A | LEU176 |
A | EDO302 |
A | HOH418 |
A | HOH433 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | LEU96 |
A | PHE127 |
A | EDO301 |
A | HOH492 |
A | ASN40 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | SER201 |
A | GLU202 |
A | VAL216 |
A | HOH470 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | TYR50 |
A | GLU109 |
A | GLY121 |
A | GLN122 |
A | PHE123 |
A | GLY124 |
A | HOH413 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | LYS142 |
A | ASN144 |
A | ASP145 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | GLN75 |
A | GLN138 |
A | ARG177 |
A | PHE179 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | ARG49 |
A | HOH410 |
A | HOH490 |
A | HOH529 |
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 | ASN40 | |
A | ASP82 | |
A | LYS101 | |
A | PHE127 | |