4ADU
Crystal structure of plasmodial PLP synthase with bound R5P intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0016843 | molecular_function | amine-lyase activity |
| A | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| A | 0042819 | biological_process | vitamin B6 biosynthetic process |
| A | 0042823 | biological_process | pyridoxal 5'-phosphate biosynthetic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0016843 | molecular_function | amine-lyase activity |
| B | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| B | 0042819 | biological_process | vitamin B6 biosynthetic process |
| B | 0042823 | biological_process | pyridoxal 5'-phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | EDO303 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | EDO302 |
| A | EDO305 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | EDO305 |
| A | EDO306 |
| A | HOH2087 |
| B | TYR176 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 305 |
| Chain | Residue |
| A | EDO306 |
| A | EDO303 |
| A | EDO304 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 306 |
| Chain | Residue |
| A | EDO304 |
| A | EDO305 |
| B | TYR176 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE R5P A 1084 |
| Chain | Residue |
| A | ASP27 |
| A | PRO52 |
| A | LYS84 |
| A | ASP105 |
| A | ALA155 |
| A | GLY156 |
| A | GLY216 |
| A | GLY217 |
| A | PHE236 |
| A | VAL237 |
| A | GLY238 |
| A | SER239 |
| A | HOH2075 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE R5P B 1084 |
| Chain | Residue |
| B | ASP27 |
| B | PRO52 |
| B | LYS84 |
| B | ASP105 |
| B | SER107 |
| B | VAL109 |
| B | ALA155 |
| B | GLY156 |
| B | GLY216 |
| B | GLY217 |
| B | GLY238 |
| B | SER239 |
| B | HOH2039 |
| B | HOH2050 |
| B | HOH2051 |
Functional Information from PROSITE/UniProt
| site_id | PS01235 |
| Number of Residues | 19 |
| Details | PDXS_SNZ_1 PdxS/SNZ family signature. LPVVNFAAGGIATPADAAM |
| Chain | Residue | Details |
| A | LEU208-MET226 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with D-ribose 5-phosphate","evidences":[{"source":"PubMed","id":"22244765","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22244765","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q03148","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
