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 | 5 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | ASN107 |
A | ATP301 |
A | HOH526 |
A | HOH536 |
A | HOH581 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 702 |
Chain | Residue |
B | HOH845 |
B | ASN107 |
B | ATP601 |
B | HOH829 |
B | HOH844 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ATP A 301 |
Chain | Residue |
A | ASN107 |
A | ALA111 |
A | ASP149 |
A | MET154 |
A | ASN162 |
A | GLY198 |
A | PHE199 |
A | THR245 |
A | MG401 |
A | HOH504 |
A | HOH505 |
A | HOH512 |
A | HOH514 |
A | HOH521 |
A | HOH532 |
A | HOH543 |
A | HOH544 |
A | HOH547 |
A | HOH581 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 501 |
Chain | Residue |
A | ILE210 |
A | THR212 |
A | ARG237 |
A | PG4503 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 A 502 |
Chain | Residue |
A | ASP235 |
A | PRO236 |
B | LYS142 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 503 |
Chain | Residue |
A | THR240 |
A | LEU241 |
A | PG4501 |
A | HOH611 |
site_id | AC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ATP B 601 |
Chain | Residue |
A | LYS95 |
B | ASN107 |
B | ALA111 |
B | ASP149 |
B | MET154 |
B | ASN162 |
B | GLY198 |
B | PHE199 |
B | THR245 |
B | MG702 |
B | HOH803 |
B | HOH811 |
B | HOH815 |
B | HOH844 |
B | HOH860 |
B | HOH872 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 B 801 |
Chain | Residue |
B | THR212 |
B | ARG237 |
B | PG4802 |
B | HOH850 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 B 802 |
Chain | Residue |
B | LYS137 |
B | HIS146 |
B | PG4801 |
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 | LYS168 | |
B | LYS168 | |
Chain | Residue | Details |
A | SER172 | |
B | SER172 | |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by CK2 => ECO:0000255 |
Chain | Residue | Details |
A | GLY288 | |
B | GLY325 | |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN107 | |
A | ASN217 | |
B | ASN107 | |
B | ASN217 | |