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 | 3 |
Details | BINDING SITE FOR RESIDUE MG B 755 |
Chain | Residue |
B | ASN107 |
B | ADP302 |
B | HOH860 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 755 |
Chain | Residue |
A | ASN107 |
A | ADP301 |
A | HOH891 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG B 756 |
Chain | Residue |
B | ASP737 |
B | GLU740 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 756 |
Chain | Residue |
B | HOH836 |
B | HOH837 |
A | ASP737 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADP A 301 |
Chain | Residue |
A | ASN107 |
A | ALA111 |
A | ASP149 |
A | MET154 |
A | ASN162 |
A | GLY198 |
A | PHE199 |
A | MG755 |
A | HOH776 |
A | HOH891 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP B 302 |
Chain | Residue |
B | ASN107 |
B | ALA111 |
B | ASP149 |
B | MET154 |
B | ASN162 |
B | GLY198 |
B | PHE199 |
B | THR245 |
B | MG755 |
B | HOH791 |
B | HOH831 |
B | HOH860 |
Functional Information from PROSITE/UniProt
site_id | PS00298 |
Number of Residues | 10 |
Details | HSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE |
Chain | Residue | Details |
A | TYR94-GLU103 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASN107 | |
B | ASN107 | |
Chain | Residue | Details |
A | ASP149 | |
A | PHE199 | |
B | ASP149 | |
B | PHE199 | |
Chain | Residue | Details |
A | ASN162 | |
B | ASN162 | |
Chain | Residue | Details |
A | ARG448 | |
B | ARG448 | |
Chain | Residue | Details |
A | LYS168 | |
B | LYS168 | |
Chain | Residue | Details |
A | SER172 | |
A | SER403 | |
B | SER172 | |
B | SER403 | |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by CK2 => ECO:0000255 |
Chain | Residue | Details |
A | GLY288 | |
B | GLY288 | |
Chain | Residue | Details |
A | TRP343 | |
B | TRP343 | |
Chain | Residue | Details |
A | LYS404 | |
A | LYS633 | |
B | LYS404 | |
B | LYS633 | |
Chain | Residue | Details |
A | SER447 | |
B | SER447 | |
Chain | Residue | Details |
A | LYS479 | |
B | LYS479 | |
site_id | SWS_FT_FI12 |
Number of Residues | 10 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN107 | |
B | ASN502 | |
A | ASN217 | |
A | ASN445 | |
A | ASN481 | |
A | ASN502 | |
B | ASN107 | |
B | ASN217 | |
B | ASN445 | |
B | ASN481 | |