6SU9
Crystal structure of Plasmodium falciparum PdxK with ligands AMP-PNP and PL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000304 | biological_process | response to singlet oxygen |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008478 | molecular_function | pyridoxal kinase activity |
| A | 0008614 | biological_process | pyridoxine metabolic process |
| A | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0042819 | biological_process | vitamin B6 biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070280 | molecular_function | pyridoxal binding |
| A | 0070281 | molecular_function | pyridoxamine binding |
| A | 0070282 | molecular_function | pyridoxine binding |
| B | 0000304 | biological_process | response to singlet oxygen |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008478 | molecular_function | pyridoxal kinase activity |
| B | 0008614 | biological_process | pyridoxine metabolic process |
| B | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0042819 | biological_process | vitamin B6 biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070280 | molecular_function | pyridoxal binding |
| B | 0070281 | molecular_function | pyridoxamine binding |
| B | 0070282 | molecular_function | pyridoxine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue ANP A 701 |
| Chain | Residue |
| A | ASP323 |
| A | GLY426 |
| A | SER427 |
| A | GLY428 |
| A | LEU454 |
| A | GLN458 |
| A | MG703 |
| A | HOH803 |
| A | HOH805 |
| A | HOH817 |
| A | HOH822 |
| A | ASN350 |
| A | HOH830 |
| A | THR386 |
| A | SER387 |
| A | LEU397 |
| A | ILE417 |
| A | ILE420 |
| A | PHE422 |
| A | PHE425 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PXL A 702 |
| Chain | Residue |
| A | SER11 |
| A | CYS18 |
| A | LYS45 |
| A | HIS48 |
| A | ASP429 |
| A | HOH817 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 703 |
| Chain | Residue |
| A | ASP318 |
| A | ANP701 |
| A | HOH805 |
| A | HOH808 |
| A | HOH822 |
| A | HOH830 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 704 |
| Chain | Residue |
| A | ARG28 |
| B | PHE25 |
| B | ARG28 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue ANP B 501 |
| Chain | Residue |
| B | ASP318 |
| B | ASP323 |
| B | ASN350 |
| B | GLU353 |
| B | THR386 |
| B | SER387 |
| B | LEU397 |
| B | LEU399 |
| B | LEU418 |
| B | LYS419 |
| B | ASN423 |
| B | SER427 |
| B | GLY428 |
| B | ASP429 |
| B | LEU454 |
| B | GLN458 |
| B | PXL502 |
| B | MG503 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue PXL B 502 |
| Chain | Residue |
| B | SER11 |
| B | CYS18 |
| B | LYS45 |
| B | HIS48 |
| B | TYR83 |
| B | ASP429 |
| B | ANP501 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | ASP318 |
| B | THR348 |
| B | PRO349 |
| B | ASN350 |
| B | THR386 |
| B | ANP501 |
