6DZG
Crystal structure of polyphosphate kinase 2 class I (SMc02148) in complex with ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006754 | biological_process | ATP biosynthetic process |
| A | 0006793 | biological_process | phosphorus metabolic process |
| A | 0008976 | molecular_function | polyphosphate kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0006754 | biological_process | ATP biosynthetic process |
| B | 0006793 | biological_process | phosphorus metabolic process |
| B | 0008976 | molecular_function | polyphosphate kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0006754 | biological_process | ATP biosynthetic process |
| C | 0006793 | biological_process | phosphorus metabolic process |
| C | 0008976 | molecular_function | polyphosphate kinase activity |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016310 | biological_process | phosphorylation |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0006754 | biological_process | ATP biosynthetic process |
| D | 0006793 | biological_process | phosphorus metabolic process |
| D | 0008976 | molecular_function | polyphosphate kinase activity |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016310 | biological_process | phosphorylation |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ADP A 401 |
| Chain | Residue |
| A | LYS97 |
| A | HOH547 |
| A | HOH564 |
| B | ASN109 |
| B | ARG111 |
| A | LYS120 |
| A | ARG149 |
| A | ASN153 |
| A | PHE163 |
| A | SER220 |
| A | MSE222 |
| A | HOH516 |
| A | HOH529 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MLT A 402 |
| Chain | Residue |
| A | ALA94 |
| A | GLY96 |
| A | LYS97 |
| A | GLY98 |
| A | GLY99 |
| A | ARG209 |
| A | LYS218 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ADP B 401 |
| Chain | Residue |
| A | ARG111 |
| B | LYS120 |
| B | ARG149 |
| B | ASN153 |
| B | VAL157 |
| B | PHE163 |
| B | SER220 |
| B | MSE222 |
| B | HOH503 |
| B | HOH509 |
| B | HOH526 |
| B | HOH536 |
| B | HOH568 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue MLT B 402 |
| Chain | Residue |
| B | ALA94 |
| B | ALA95 |
| B | GLY96 |
| B | LYS97 |
| B | GLY98 |
| B | GLY99 |
| B | ARG209 |
| B | LYS218 |
| B | HOH571 |
| B | HOH580 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue MLT B 403 |
| Chain | Residue |
| B | GLU59 |
| B | ARG261 |
| B | ARG268 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue ADP C 401 |
| Chain | Residue |
| C | LYS120 |
| C | ARG149 |
| C | ASN153 |
| C | PHE163 |
| C | SER220 |
| C | MSE222 |
| C | HOH510 |
| C | HOH534 |
| C | HOH547 |
| C | HOH576 |
| D | ASN109 |
| D | ARG111 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MLT C 402 |
| Chain | Residue |
| C | ALA94 |
| C | GLY96 |
| C | LYS97 |
| C | GLY98 |
| C | GLY99 |
| C | ARG209 |
| C | LYS218 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue AMP D 401 |
| Chain | Residue |
| C | ARG111 |
| D | LYS120 |
| D | ARG149 |
| D | ASN153 |
| D | PHE163 |
| D | SER220 |
| D | MSE222 |
| D | HOH550 |
| D | HOH559 |
| D | HOH560 |
| D | HOH570 |
| D | HOH613 |
| D | HOH622 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MLT D 402 |
| Chain | Residue |
| D | ALA94 |
| D | GLY96 |
| D | LYS97 |
| D | GLY98 |
| D | GLY99 |
| D | ARG209 |
| D | LYS218 |
