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 | 12 |
Details | binding site for residue ACP A 401 |
Chain | Residue |
A | GLY196 |
A | GLY342 |
A | GLN343 |
A | HOH522 |
A | GLY197 |
A | GLY198 |
A | THR199 |
A | GLU267 |
A | LYS270 |
A | ILE271 |
A | SER274 |
A | GLY341 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue ACP B 401 |
Chain | Residue |
A | HOH507 |
B | GLY197 |
B | GLY198 |
B | THR199 |
B | GLU267 |
B | LYS270 |
B | ILE271 |
B | SER274 |
B | GLY342 |
B | GLN343 |
B | ARG345 |
B | HOH510 |
Functional Information from PROSITE/UniProt
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSII |
Chain | Residue | Details |
A | VAL192-ILE205 | |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGqTRMPmVqK |
Chain | Residue | Details |
A | VAL337-LYS351 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR199 | |
B | THR199 | |
Chain | Residue | Details |
A | LYS245 | |
A | LYS304 | |
B | LYS245 | |
B | LYS304 | |
Chain | Residue | Details |
A | LYS246 | |
A | LYS359 | |
B | LYS246 | |
B | LYS359 | |