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 | 14 |
Details | BINDING SITE FOR RESIDUE N5A A 401 |
Chain | Residue |
A | ALA111 |
A | HOH509 |
A | HOH514 |
A | HOH540 |
A | HOH543 |
A | HOH565 |
A | ASP149 |
A | MET154 |
A | ASN162 |
A | GLY196 |
A | VAL197 |
A | THR245 |
A | HOH507 |
A | HOH508 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE N5A B 402 |
Chain | Residue |
B | ALA111 |
B | ASP149 |
B | MET154 |
B | ASN162 |
B | LEU163 |
B | GLY196 |
B | TYR200 |
B | THR245 |
B | HOH602 |
B | HOH603 |
B | HOH605 |
B | HOH606 |
B | HOH650 |
B | HOH659 |
B | HOH679 |
B | HOH693 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PG4 A 501 |
Chain | Residue |
A | THR212 |
A | ARG237 |
A | THR240 |
A | THR246 |
A | THR248 |
A | HOH530 |
A | HOH538 |
A | HOH559 |
A | HOH589 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 A 502 |
Chain | Residue |
A | LYS137 |
A | TRP282 |
A | HOH510 |
A | HOH517 |
A | HOH561 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PG4 B 503 |
Chain | Residue |
B | THR212 |
B | ARG237 |
B | THR240 |
B | THR246 |
B | THR248 |
B | HOH607 |
B | HOH626 |
B | HOH631 |
B | HOH666 |
B | HOH690 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PG4 B 504 |
Chain | Residue |
B | LYS137 |
B | HOH633 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PG4 A 505 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE B 601 |
Chain | Residue |
A | ASN83 |
A | LYS87 |
A | ILE90 |
A | SER227 |
B | ASN83 |
B | LYS87 |
B | ILE90 |
B | SER227 |
B | HOH628 |
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 | GLY288 | |
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 | |