3HY8
Crystal Structure of Human Pyridoxine 5'-Phosphate Oxidase R229W Mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0042818 | biological_process | pyridoxamine metabolic process |
| A | 0042822 | biological_process | pyridoxal phosphate metabolic process |
| A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| A | 1901615 | biological_process | organic hydroxy compound metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN A 390 |
| Chain | Residue |
| A | ARG95 |
| A | TYR132 |
| A | GLN139 |
| A | ARG141 |
| A | GLN174 |
| A | TRP219 |
| A | TRP229 |
| A | HOH308 |
| A | PLP350 |
| A | PO4370 |
| A | MET96 |
| A | LEU97 |
| A | LEU98 |
| A | PHE110 |
| A | THR111 |
| A | SER115 |
| A | ARG116 |
| A | LYS117 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP A 350 |
| Chain | Residue |
| A | GLU77 |
| A | LEU98 |
| A | LYS100 |
| A | ARG161 |
| A | PRO162 |
| A | SER165 |
| A | TRP219 |
| A | ARG225 |
| A | HIS227 |
| A | FMN390 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 360 |
| Chain | Residue |
| A | LYS100 |
| A | GLY101 |
| A | ARG108 |
| A | PHE110 |
| A | GLU153 |
| A | TYR157 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 370 |
| Chain | Residue |
| A | ARG116 |
| A | ARG141 |
| A | GLU143 |
| A | GLU217 |
| A | TRP229 |
| A | FMN390 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 380 |
| Chain | Residue |
| A | SER55 |
| A | LYS60 |
| A | LYS60 |
| A | GLU251 |
| A | HOH297 |
| A | HOH320 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0AFI7 |
| Chain | Residue | Details |
| A | ARG42 | |
| A | GLN139 | |
| A | TRP219 | |
| A | ARG225 | |
| A | TRP229 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12824491 |
| Chain | Residue | Details |
| A | ARG95 | |
| A | LYS100 | |
| A | PHE110 | |
| A | ARG116 | |
| A | TYR157 | |
| A | ARG161 | |
| A | SER165 | |
| A | GLN174 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR238 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER241 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g79 |
| Chain | Residue | Details |
| A | ARG225 |
