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 | 27 |
Details | BINDING SITE FOR RESIDUE AGS A 301 |
Chain | Residue |
A | GLU47 |
A | VAL136 |
A | GLY137 |
A | PHE138 |
A | THR184 |
A | MG401 |
A | HOH502 |
A | HOH503 |
A | HOH506 |
A | HOH510 |
A | HOH513 |
A | ASN51 |
A | HOH520 |
A | HOH569 |
A | HOH571 |
A | HOH578 |
A | HOH659 |
A | HOH681 |
A | HOH692 |
A | HOH721 |
A | ALA55 |
A | ASP93 |
A | MET98 |
A | ASN106 |
A | LEU107 |
A | GLY132 |
A | GLY135 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | ASN51 |
A | AGS301 |
A | HOH503 |
A | HOH513 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE AGS B 301 |
Chain | Residue |
B | ASN51 |
B | ALA55 |
B | ASP93 |
B | MET98 |
B | ASN106 |
B | LEU107 |
B | GLY135 |
B | VAL136 |
B | GLY137 |
B | PHE138 |
B | THR184 |
B | MG401 |
B | HOH501 |
B | HOH505 |
B | HOH506 |
B | HOH508 |
B | HOH552 |
B | HOH595 |
B | HOH621 |
B | HOH681 |
B | HOH700 |
B | HOH710 |
B | HOH711 |
B | HOH712 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | ASN51 |
B | AGS301 |
B | HOH505 |
B | HOH711 |
B | HOH712 |
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: |
Chain | Residue | Details |
A | ASN51 | |
A | ASP93 | |
A | PHE138 | |
B | ASN51 | |
B | ASP93 | |
B | PHE138 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS112 | |
B | LYS112 | |
Chain | Residue | Details |
A | LYS58 | |
A | LYS84 | |
B | LYS58 | |
B | LYS84 | |
Chain | Residue | Details |
A | SER231 | |
B | SER231 | |