1JNW
Active Site Structure of E. coli pyridoxine 5'-phosphate Oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| 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 | 0032991 | cellular_component | protein-containing complex |
| A | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| A | 0042301 | molecular_function | phosphate ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| A | 1902444 | molecular_function | riboflavin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 270 |
| Chain | Residue |
| A | ARG23 |
| A | ARG24 |
| A | ALA152 |
| A | ARG153 |
| A | PHE202 |
| A | ARG215 |
| A | HOH399 |
| A | HOH400 |
| A | HOH507 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN A 250 |
| Chain | Residue |
| A | TYR17 |
| A | ARG67 |
| A | ILE68 |
| A | VAL69 |
| A | LEU70 |
| A | TYR82 |
| A | THR83 |
| A | SER87 |
| A | ARG88 |
| A | LYS89 |
| A | GLN111 |
| A | GLN146 |
| A | SER147 |
| A | TRP191 |
| A | ARG201 |
| A | PLP260 |
| A | HOH348 |
| A | HOH375 |
| A | HOH407 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP A 260 |
| Chain | Residue |
| A | ARG14 |
| A | TYR17 |
| A | LYS72 |
| A | TYR129 |
| A | ARG133 |
| A | ARG197 |
| A | HIS199 |
| A | PRO218 |
| A | FMN250 |
| A | HOH408 |
Functional Information from PROSITE/UniProt
| site_id | PS01064 |
| Number of Residues | 14 |
| Details | PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. IEFWQggehRLHDR |
| Chain | Residue | Details |
| A | ILE188-ARG201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11786019 |
| Chain | Residue | Details |
| A | ARG15 | |
| A | LEU198 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270 |
| Chain | Residue | Details |
| A | ILE68 | |
| A | THR83 | |
| A | LYS89 | |
| A | ALA90 | |
| A | SER147 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11453690 |
| Chain | Residue | Details |
| A | HIS73 | |
| A | PHE130 | |
| A | PRO134 | |
| A | GLN138 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270 |
| Chain | Residue | Details |
| A | VAL112 | |
| A | PHE202 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15858270 |
| Chain | Residue | Details |
| A | GLN192 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g79 |
| Chain | Residue | Details |
| A | ARG197 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 677 |
| Chain | Residue | Details |
| A | ALA217 | steric role |
