6H00
Crystal structure of human pyridoxine 5-phophate oxidase, R116Q variant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| 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 | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| 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 | 4 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | LYS100 |
| A | ARG161 |
| A | SER165 |
| A | ARG225 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | HOH434 |
| A | GLN71 |
| A | VAL170 |
| A | VAL171 |
| A | SER172 |
| A | HIS173 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | THR247 |
| A | HIS248 |
| A | ARG249 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue FMN A 304 |
| Chain | Residue |
| A | GLU77 |
| A | ARG95 |
| A | MET96 |
| A | LEU97 |
| A | LEU98 |
| A | PHE110 |
| A | THR111 |
| A | SER115 |
| A | GLN116 |
| A | LYS117 |
| A | TYR132 |
| A | GLN139 |
| A | ARG141 |
| A | GLN174 |
| A | SER175 |
| A | TRP219 |
| A | ARG229 |
| A | HOH401 |
| A | HOH412 |
| A | HOH419 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | LEU121 |
| A | ASP122 |
| A | VAL146 |
| A | LYS147 |
| A | LYS148 |
| A | EDO306 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | LYS148 |
| A | EDO305 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | HIS52 |
| A | LEU53 |
| A | THR54 |
| A | GLN61 |
| A | TRP65 |
| A | ARG138 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 308 |
| Chain | Residue |
| A | GLU77 |
| A | ALA78 |
| A | ALA80 |
| A | TYR132 |
| A | TYR132 |
| A | TRP133 |
| A | GLU134 |
Functional Information from PROSITE/UniProt
| site_id | PS01064 |
| Number of Residues | 14 |
| Details | PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. MEFWQgqtnRLHDR |
| Chain | Residue | Details |
| A | MET216-ARG229 |
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 | ARG229 |
| 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 | GLN116 | |
| 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 |
