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 |