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 |
| 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 |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006457 | biological_process | protein folding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue AGS A 600 |
| Chain | Residue |
| A | THR121 |
| A | ARG370 |
| B | ARG307 |
| A | GLY122 |
| A | SER123 |
| A | GLY124 |
| A | LYS125 |
| A | THR126 |
| A | LEU127 |
| A | GLN185 |
| A | ALA369 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue AGS B 600 |
| Chain | Residue |
| B | ILE79 |
| B | GLN81 |
| B | GLY122 |
| B | SER123 |
| B | GLY124 |
| B | LYS125 |
| B | THR126 |
| B | LEU127 |
| B | ILE325 |
| B | ARG370 |
| C | GLU303 |
| C | ARG307 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue AGS C 600 |
| Chain | Residue |
| C | VAL78 |
| C | ILE79 |
| C | PRO120 |
| C | GLY122 |
| C | SER123 |
| C | GLY124 |
| C | LYS125 |
| C | THR126 |
| C | LEU127 |
| C | ILE325 |
| C | ALA369 |
| C | ARG370 |
| D | GLU109 |
| D | ARG307 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue AGS D 600 |
| Chain | Residue |
| D | VAL78 |
| D | ILE79 |
| D | PRO120 |
| D | GLY122 |
| D | SER123 |
| D | GLY124 |
| D | LYS125 |
| D | THR126 |
| D | LEU127 |
| D | GLN185 |
| D | ILE325 |
| D | ALA369 |
| D | ARG370 |
| E | GLU303 |
| E | ARG307 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue ADP F 600 |
| Chain | Residue |
| F | TYR77 |
| F | VAL78 |
| F | ILE79 |
| F | PRO120 |
| F | THR121 |
| F | GLY122 |
| F | SER123 |
| F | GLY124 |
| F | LYS125 |
| F | THR126 |
| F | LEU127 |
| F | TYR182 |
| F | ASP184 |
| F | ILE325 |
| F | ALA369 |
| F | ARG370 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide AGS E 600 and SER E 123 |
| Chain | Residue |
| E | ILE79 |
| E | GLN81 |
| E | PRO120 |
| E | THR121 |
| E | GLY122 |
| E | GLY124 |
| E | LYS125 |
| E | THR126 |
| E | LEU127 |
| E | GLN185 |
| E | ILE325 |
| E | ALA369 |
| E | ARG370 |
| F | ARG307 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | PRO120 | |
| B | PRO120 | |
| C | PRO120 | |
| D | PRO120 | |
| E | PRO120 | |
| F | PRO120 | |
