5LL0
Structure of Polyphosphate Kinase 2 from Francisella tularensis SCHU S4 with polyphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006793 | biological_process | phosphorus metabolic process |
| A | 0008976 | molecular_function | polyphosphate kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0006793 | biological_process | phosphorus metabolic process |
| B | 0008976 | molecular_function | polyphosphate kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0006793 | biological_process | phosphorus metabolic process |
| C | 0008976 | molecular_function | polyphosphate kinase activity |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0006793 | biological_process | phosphorus metabolic process |
| D | 0008976 | molecular_function | polyphosphate kinase activity |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue 9PI A 301 |
| Chain | Residue |
| A | ARG26 |
| A | ARG72 |
| A | ARG178 |
| A | LYS184 |
| A | LYS187 |
| A | LYS228 |
| A | LYS229 |
| A | ARG232 |
| A | HOH402 |
| A | HOH457 |
| A | TYR29 |
| A | GLU30 |
| A | LYS33 |
| A | ALA63 |
| A | GLY65 |
| A | LYS66 |
| A | GLY67 |
| A | GLY68 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue 9PI B 301 |
| Chain | Residue |
| B | ARG26 |
| B | TYR29 |
| B | GLU30 |
| B | LYS33 |
| B | ALA63 |
| B | ALA64 |
| B | GLY65 |
| B | LYS66 |
| B | GLY67 |
| B | GLY68 |
| B | ARG72 |
| B | ARG178 |
| B | LYS184 |
| B | LYS187 |
| B | LYS228 |
| B | LYS229 |
| B | ARG232 |
| B | HOH408 |
| B | HOH412 |
| B | HOH419 |
| B | HOH436 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue 9PI C 301 |
| Chain | Residue |
| C | ARG26 |
| C | TYR29 |
| C | GLU30 |
| C | LYS33 |
| C | ALA63 |
| C | ALA64 |
| C | GLY65 |
| C | LYS66 |
| C | GLY67 |
| C | GLY68 |
| C | ARG72 |
| C | ARG178 |
| C | LYS184 |
| C | LYS187 |
| C | LYS228 |
| C | ARG232 |
| C | HOH403 |
| C | HOH404 |
| C | HOH446 |
| C | HOH448 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue 9PI D 301 |
| Chain | Residue |
| D | ARG26 |
| D | TYR29 |
| D | GLU30 |
| D | LYS33 |
| D | ALA63 |
| D | ALA64 |
| D | GLY65 |
| D | LYS66 |
| D | GLY67 |
| D | GLY68 |
| D | ARG72 |
| D | ARG178 |
| D | LYS184 |
| D | LYS187 |
| D | LYS228 |
| D | LYS229 |
| D | ARG232 |
| D | HOH413 |
| D | HOH424 |
| D | HOH440 |
| D | HOH481 |
| D | HOH524 |






