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 501 |
Chain | Residue |
A | ASN107 |
A | ADP301 |
A | HOH517 |
A | HOH520 |
A | HOH545 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 802 |
Chain | Residue |
B | HOH825 |
B | ASN107 |
B | ADP601 |
B | HOH823 |
B | HOH824 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ADP A 301 |
Chain | Residue |
A | ASN107 |
A | ALA111 |
A | ASP149 |
A | MET154 |
A | ASN162 |
A | LEU163 |
A | ILE166 |
A | GLY198 |
A | PHE199 |
A | THR245 |
A | MG501 |
A | HOH502 |
A | HOH503 |
A | HOH506 |
A | HOH514 |
A | HOH541 |
A | HOH545 |
A | HOH546 |
A | HOH580 |
A | HOH581 |
A | HOH606 |
A | HOH616 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 A 401 |
Chain | Residue |
A | ILE210 |
A | THR212 |
A | ARG237 |
A | PG4403 |
A | HOH624 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 402 |
Chain | Residue |
A | ASN239 |
A | THR240 |
A | GLY242 |
A | HOH529 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 A 403 |
Chain | Residue |
A | LEU241 |
A | PG4401 |
A | HOH549 |
site_id | AC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP B 601 |
Chain | Residue |
A | LYS95 |
B | ASN107 |
B | ALA111 |
B | ASP149 |
B | MET154 |
B | ASN162 |
B | GLY198 |
B | PHE199 |
B | THR245 |
B | MG802 |
B | HOH812 |
B | HOH813 |
B | HOH824 |
B | HOH825 |
B | HOH831 |
B | HOH835 |
B | HOH841 |
B | HOH857 |
B | HOH899 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 B 701 |
Chain | Residue |
B | LYS137 |
B | TRP333 |
B | HOH851 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 B 702 |
Chain | Residue |
B | LYS137 |
B | HIS146 |
B | THR148 |
B | THR246 |
B | HOH827 |
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 | |