1WV4
X-ray Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in tetragonal crystal form
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 |
| B | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0036001 | biological_process | 'de novo' pyridoxal 5'-phosphate biosynthetic process |
| B | 0042301 | molecular_function | phosphate ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| B | 1902444 | molecular_function | riboflavin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 275 |
| Chain | Residue |
| A | ARG24 |
| A | ARG215 |
| A | HOH317 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1275 |
| Chain | Residue |
| B | ARG23 |
| B | ARG24 |
| B | ARG25 |
| B | ARG215 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FMN A 250 |
| Chain | Residue |
| A | ILE68 |
| A | LEU70 |
| A | LYS72 |
| A | TYR82 |
| A | THR83 |
| A | SER87 |
| A | ARG88 |
| A | LYS89 |
| A | HOH291 |
| B | HIS106 |
| B | GLN111 |
| B | TRP191 |
| B | ARG201 |
| A | ASP49 |
| A | ARG67 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FMN B 1250 |
| Chain | Residue |
| A | GLN111 |
| A | TRP191 |
| A | ARG201 |
| B | ASP49 |
| B | ARG67 |
| B | ILE68 |
| B | VAL69 |
| B | LEU70 |
| B | TYR82 |
| B | THR83 |
| B | SER87 |
| B | ARG88 |
| B | LYS89 |
| B | HOH1282 |
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 | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11786019","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| 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_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11453690","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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_FI5 |
| Number of Residues | 2 |
| 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 | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g79 |
| Chain | Residue | Details |
| B | ARG197 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 677 |
| Chain | Residue | Details |
| A | ARG197 | steric role |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 677 |
| Chain | Residue | Details |
| B | ARG197 | steric role |
