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 | 1901615 | biological_process | organic hydroxy compound metabolic 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 | 1901615 | biological_process | organic hydroxy compound metabolic 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 | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11786019 |
Chain | Residue | Details |
A | ARG15 | |
A | LEU198 | |
B | ARG15 | |
B | LEU198 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270 |
Chain | Residue | Details |
A | ILE68 | |
B | SER147 | |
A | THR83 | |
A | LYS89 | |
A | ALA90 | |
A | SER147 | |
B | ILE68 | |
B | THR83 | |
B | LYS89 | |
B | ALA90 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11453690 |
Chain | Residue | Details |
A | HIS73 | |
A | PHE130 | |
A | PRO134 | |
A | GLN138 | |
B | HIS73 | |
B | PHE130 | |
B | PRO134 | |
B | GLN138 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270 |
Chain | Residue | Details |
A | VAL112 | |
A | PHE202 | |
B | VAL112 | |
B | PHE202 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15858270 |
Chain | Residue | Details |
A | GLN192 | |
B | 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 | 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 | LEU198 | steric role |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 677 |
Chain | Residue | Details |
B | LEU198 | steric role |