Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
B | 0005524 | molecular_function | ATP binding |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | binding site for residue ADP A 450 |
Chain | Residue |
A | THR42 |
A | SER306 |
A | GLY369 |
A | GLY370 |
A | SER371 |
A | ARG373 |
A | ILE374 |
A | ASP397 |
A | MG451 |
A | HOH501 |
A | HOH525 |
A | THR43 |
A | HOH526 |
A | HOH550 |
A | HOH575 |
A | HOH585 |
A | HOH603 |
A | TYR44 |
A | GLY231 |
A | GLY232 |
A | GLY260 |
A | GLU299 |
A | LYS302 |
A | ARG303 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 451 |
Chain | Residue |
A | ASP39 |
A | TYR44 |
A | ADP450 |
A | HOH525 |
A | HOH599 |
site_id | AC3 |
Number of Residues | 19 |
Details | binding site for residue ADP B 450 |
Chain | Residue |
B | THR42 |
B | THR43 |
B | TYR44 |
B | GLY232 |
B | GLY260 |
B | GLU299 |
B | LYS302 |
B | ARG303 |
B | SER306 |
B | GLY369 |
B | GLY370 |
B | SER371 |
B | ARG373 |
B | ASP397 |
B | MG452 |
B | HOH501 |
B | HOH533 |
B | HOH542 |
B | HOH587 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MG B 452 |
Chain | Residue |
B | ASP39 |
B | TYR44 |
B | ADP450 |
B | HOH533 |
Functional Information from PROSITE/UniProt
site_id | PS00297 |
Number of Residues | 8 |
Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
Chain | Residue | Details |
A | ILE38-SER45 | |
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. IFDLGGGTfdvSLL |
Chain | Residue | Details |
A | ILE227-LEU240 | |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ |
Chain | Residue | Details |
A | ILE365-GLN379 | |