1G77
X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006725 | biological_process | cellular aromatic compound metabolic process |
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 | 1901615 | biological_process | organic hydroxy compound metabolic 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 280 |
Chain | Residue |
A | ARG23 |
A | ARG24 |
A | ARG120 |
A | ALA152 |
A | ARG153 |
A | ARG215 |
A | HOH310 |
A | HOH329 |
A | HOH336 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 A 290 |
Chain | Residue |
A | SER148 |
A | ARG149 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE FMN A 250 |
Chain | Residue |
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 | HOH308 |
A | HOH312 |
A | HOH322 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PLP A 260 |
Chain | Residue |
A | LYS72 |
A | TYR129 |
A | ARG133 |
A | GLN146 |
A | ARG197 |
A | HIS199 |
A | PRO218 |
A | FMN250 |
A | HOH338 |
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 | ARG14 | |
A | ARG197 |
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 | ARG67 | |
A | TYR82 | |
A | ARG88 | |
A | LYS89 | |
A | GLN146 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11453690 |
Chain | Residue | Details |
A | LYS72 | |
A | TYR129 | |
A | ARG133 | |
A | SER137 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270 |
Chain | Residue | Details |
A | GLN111 | |
A | ARG201 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15858270 |
Chain | Residue | Details |
A | TRP191 |
Catalytic Information from CSA