Functional Information from GO Data
Chain | GOid | namespace | contents |
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 |
C | 0005524 | molecular_function | ATP binding |
C | 0006457 | biological_process | protein folding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0051082 | molecular_function | unfolded protein binding |
C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 401 |
Chain | Residue |
C | LYS135 |
C | TRP333 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 402 |
Chain | Residue |
C | LYS214 |
C | ASN217 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue EQD C 403 |
Chain | Residue |
C | THR245 |
C | ILE247 |
C | HOH502 |
C | HOH503 |
C | HOH510 |
C | ALA111 |
C | ASP149 |
C | MET154 |
C | ASN162 |
C | PHE195 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO C 404 |
Chain | Residue |
B | VAL250 |
C | THR219 |
C | GLN220 |
C | ASP235 |
C | GLY238 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO C 405 |
Chain | Residue |
B | EDO408 |
C | EDO406 |
C | HOH504 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO C 406 |
Chain | Residue |
C | ASN96 |
C | TYR271 |
C | EDO405 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 401 |
Chain | Residue |
B | LYS214 |
B | ASN216 |
B | ASN217 |
B | ASP218 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 402 |
Chain | Residue |
B | LYS135 |
B | TRP333 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 403 |
Chain | Residue |
B | THR219 |
B | HIS221 |
B | ALA234 |
C | LYS208 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 404 |
Chain | Residue |
B | HIS215 |
B | ASN217 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue EQD B 405 |
Chain | Residue |
B | ALA111 |
B | ASP149 |
B | ASN162 |
B | PHE195 |
B | THR245 |
B | ILE247 |
B | HOH503 |
B | HOH505 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue EDO B 406 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 407 |
Chain | Residue |
B | HIS146 |
B | THR212 |
B | ARG237 |
B | EDO406 |
C | PRO236 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 408 |
Chain | Residue |
B | HOH507 |
C | EDO405 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue EDO B 409 |
Chain | Residue |
B | LYS208 |
C | HIS221 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue EDO B 410 |
Chain | Residue |
B | GLU224 |
B | GLU229 |
C | ARG156 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue EDO B 411 |
Chain | Residue |
B | TRP282 |
B | HOH504 |
Functional Information from PROSITE/UniProt
site_id | PS00298 |
Number of Residues | 10 |
Details | HSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE |
Chain | Residue | Details |
C | TYR94-GLU103 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
C | ASN107 | |
B | ASN107 | |
Chain | Residue | Details |
C | ASP149 | |
C | PHE199 | |
B | ASP149 | |
B | PHE199 | |
Chain | Residue | Details |
C | ASN162 | |
B | ASN162 | |
Chain | Residue | Details |
C | LYS168 | |
B | LYS168 | |
Chain | Residue | Details |
C | SER172 | |
B | SER172 | |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
C | ASN107 | |
C | ASN217 | |
B | ASN107 | |
B | ASN217 | |