5LLB
Structure of Polyphosphate Kinase 2 from Francisella tularensis with AMPPCH2PPP and 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 | 3 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | ARG61 |
| A | TRP163 |
| A | SER165 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP62 |
| A | ASP192 |
| A | 6YZ303 |
| A | HOH401 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue 6YZ A 303 |
| Chain | Residue |
| A | GLY65 |
| A | LYS66 |
| A | GLY67 |
| A | LEU87 |
| A | LYS89 |
| A | ARG118 |
| A | ASN122 |
| A | VAL126 |
| A | PHE132 |
| A | ARG178 |
| A | SER189 |
| A | ILE191 |
| A | ASP192 |
| A | MG302 |
| A | HOH401 |
| A | HOH403 |
| A | HOH420 |
| A | HOH425 |
| A | HOH463 |
| A | HOH472 |
| A | HOH504 |
| A | ALA63 |
| A | ALA64 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue 6YW A 304 |
| Chain | Residue |
| A | TYR29 |
| A | LYS33 |
| A | ARG72 |
| A | LYS184 |
| A | LYS187 |
| A | LYS228 |
| A | ARG232 |
| A | HOH464 |
| A | HOH472 |
| A | HOH477 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 301 |
| Chain | Residue |
| B | ARG61 |
| B | TRP163 |
| B | SER165 |
| B | LYS206 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | ASP62 |
| B | ASP192 |
| B | 6YZ303 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue 6YZ B 303 |
| Chain | Residue |
| B | ALA63 |
| B | ALA64 |
| B | GLY65 |
| B | LYS66 |
| B | GLY67 |
| B | LYS89 |
| B | PRO90 |
| B | ARG118 |
| B | ASN122 |
| B | VAL126 |
| B | PHE132 |
| B | ARG178 |
| B | LYS187 |
| B | SER189 |
| B | ILE191 |
| B | MG302 |
| B | HOH403 |
| B | HOH404 |
| B | HOH434 |
| B | HOH468 |
| B | HOH473 |
| B | HOH494 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue 6YW B 304 |
| Chain | Residue |
| B | ARG26 |
| B | TYR29 |
| B | GLU30 |
| B | LYS33 |
| B | ARG72 |
| B | LYS184 |
| B | LYS187 |
| B | LYS228 |
| B | LYS229 |
| B | ARG232 |
| B | HOH402 |
| B | HOH403 |
| B | HOH461 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 301 |
| Chain | Residue |
| C | ARG61 |
| C | TRP163 |
| C | SER165 |
| C | LYS206 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 302 |
| Chain | Residue |
| C | ASP62 |
| C | ASP192 |
| C | 6YZ303 |
| C | HOH410 |
| site_id | AD2 |
| Number of Residues | 27 |
| Details | binding site for residue 6YZ C 303 |
| Chain | Residue |
| C | ASN122 |
| C | VAL126 |
| C | PHE132 |
| C | ARG178 |
| C | SER189 |
| C | ILE191 |
| C | ASP192 |
| C | MG302 |
| C | HOH403 |
| C | HOH405 |
| C | HOH410 |
| C | HOH414 |
| C | HOH428 |
| C | HOH434 |
| C | HOH436 |
| C | HOH455 |
| C | HOH506 |
| C | HOH546 |
| C | ASP62 |
| C | ALA63 |
| C | ALA64 |
| C | GLY65 |
| C | LYS66 |
| C | GLY67 |
| C | GLU88 |
| C | LYS89 |
| C | ARG118 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue 6YW C 304 |
| Chain | Residue |
| C | ARG26 |
| C | TYR29 |
| C | GLU30 |
| C | LYS33 |
| C | ARG72 |
| C | LYS184 |
| C | LYS228 |
| C | LYS229 |
| C | ARG232 |
| C | HOH455 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 301 |
| Chain | Residue |
| D | ARG61 |
| D | TRP163 |
| D | SER165 |
| D | LYS206 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 302 |
| Chain | Residue |
| D | ASP62 |
| D | ASP192 |
| D | 6YZ303 |
| D | HOH405 |
| site_id | AD6 |
| Number of Residues | 24 |
| Details | binding site for residue 6YZ D 303 |
| Chain | Residue |
| D | ASP62 |
| D | ALA63 |
| D | ALA64 |
| D | GLY65 |
| D | LYS66 |
| D | GLY67 |
| D | LYS89 |
| D | ARG118 |
| D | ASN122 |
| D | VAL126 |
| D | PHE132 |
| D | ARG178 |
| D | SER189 |
| D | ILE191 |
| D | ASP192 |
| D | MG302 |
| D | HOH405 |
| D | HOH408 |
| D | HOH411 |
| D | HOH427 |
| D | HOH439 |
| D | HOH455 |
| D | HOH456 |
| D | HOH462 |
| site_id | AD7 |
| Number of Residues | 11 |
| Details | binding site for residue 6YW D 304 |
| Chain | Residue |
| D | ARG26 |
| D | TYR29 |
| D | GLU30 |
| D | GLY68 |
| D | ARG72 |
| D | LYS184 |
| D | LYS187 |
| D | LYS228 |
| D | LYS229 |
| D | ARG232 |
| D | HOH462 |
