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 | 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 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 | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10903950","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11453690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11453690","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11786019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15858270","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
