1T9M
X-ray crystal structure of phzG from pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| A | 0006725 | biological_process | obsolete 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 | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| A | 1901615 | biological_process | organic hydroxy compound metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| B | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
| 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 | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| B | 1901615 | biological_process | organic hydroxy compound metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 351 |
| Chain | Residue |
| A | ARG39 |
| A | GLN59 |
| A | ARG61 |
| B | HOH748 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 352 |
| Chain | Residue |
| A | ARG118 |
| A | ARG170 |
| A | PRO172 |
| A | GLY173 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 353 |
| Chain | Residue |
| B | ARG170 |
| B | PRO172 |
| B | GLY173 |
| B | HOH721 |
| B | ARG118 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 354 |
| Chain | Residue |
| A | ARG41 |
| A | ARG42 |
| B | PRO95 |
| B | TRP96 |
| B | ARG115 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN A 250 |
| Chain | Residue |
| A | ARG65 |
| A | ILE66 |
| A | VAL67 |
| A | VAL68 |
| A | ALA80 |
| A | THR81 |
| A | SER85 |
| A | GLN86 |
| A | LYS87 |
| A | GLN144 |
| A | SER145 |
| A | HOH420 |
| A | HOH421 |
| A | HOH427 |
| A | HOH431 |
| A | HOH487 |
| B | TYR102 |
| B | GLN109 |
| B | TRP187 |
| B | ARG197 |
| B | HOH405 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN B 350 |
| Chain | Residue |
| A | TYR102 |
| A | GLN109 |
| A | TRP187 |
| A | ARG197 |
| A | HOH403 |
| A | HOH670 |
| B | ARG65 |
| B | ILE66 |
| B | VAL67 |
| B | VAL68 |
| B | ALA80 |
| B | THR81 |
| B | SER85 |
| B | GLN86 |
| B | LYS87 |
| B | GLN144 |
| B | SER145 |
| B | HOH408 |
| B | HOH430 |
| B | HOH444 |
| B | HOH446 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY B 301 |
| Chain | Residue |
| A | TYR102 |
| A | ARG104 |
| A | HOH452 |
| B | TYR102 |
| B | ARG104 |
| B | HOH552 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 302 |
| Chain | Residue |
| A | ARG46 |
| A | GLU105 |
| A | HOH402 |
| B | GLU105 |
| B | HOH412 |
Functional Information from PROSITE/UniProt
| site_id | PS01064 |
| Number of Residues | 14 |
| Details | PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. VEFWGngteRLHER |
| Chain | Residue | Details |
| A | VAL184-ARG197 |
