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 | 15 |
Details | BINDING SITE FOR RESIDUE 94M A 214 |
Chain | Residue |
A | ASN36 |
A | TYR124 |
A | VAL135 |
A | THR169 |
A | HOH215 |
A | HOH221 |
A | HOH280 |
A | SER37 |
A | ALA40 |
A | ASP78 |
A | ILE81 |
A | GLY82 |
A | MET83 |
A | LEU88 |
A | PHE123 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 94M B 214 |
Chain | Residue |
B | ASN36 |
B | ALA40 |
B | ASP78 |
B | ILE81 |
B | GLY82 |
B | MET83 |
B | LEU88 |
B | LEU92 |
B | PHE123 |
B | TYR124 |
B | HOH216 |
B | HOH223 |
B | HOH251 |
B | HOH292 |
B | 1PE1300 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 1PE B 1300 |
Chain | Residue |
B | ASN36 |
B | ASP39 |
B | ALA40 |
B | ILE81 |
B | 94M214 |
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 | TYR23-GLU32 | |