1TY9
X-RAY CRYSTAL STRUCTURE OF PHZG FROM PSEUDOMONAS FLUORESCENS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002047 | biological_process | phenazine biosynthetic process |
A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
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 | 0017000 | biological_process | antibiotic biosynthetic process |
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 | 0002047 | biological_process | phenazine biosynthetic process |
B | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
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 | 0017000 | biological_process | antibiotic biosynthetic process |
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 B 261 |
Chain | Residue |
B | ARG57 |
B | SER78 |
B | GLU79 |
B | ILE80 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 262 |
Chain | Residue |
A | ARG126 |
A | ASN129 |
A | ARG178 |
A | GLU180 |
A | GLY181 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 265 |
Chain | Residue |
B | ARG126 |
B | ASN129 |
B | ARG178 |
B | PRO179 |
B | GLU180 |
B | GLY181 |
B | HOH698 |
B | HOH699 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 266 |
Chain | Residue |
B | HIS90 |
B | ALA91 |
B | GLY92 |
B | ARG151 |
B | GLN152 |
B | GLU180 |
B | GLY181 |
B | HOH482 |
B | HOH599 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FMN A 251 |
Chain | Residue |
A | ARG73 |
A | ILE74 |
A | VAL75 |
A | VAL76 |
A | SER88 |
A | THR89 |
A | SER93 |
A | GLN94 |
A | LYS95 |
A | GLN152 |
A | SER153 |
A | HOH333 |
A | HOH366 |
A | HOH390 |
A | HOH448 |
A | HOH709 |
B | LEU19 |
B | TYR110 |
B | GLN117 |
B | TRP195 |
B | ARG205 |
B | HOH364 |
site_id | AC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FMN B 252 |
Chain | Residue |
A | TYR110 |
A | GLN117 |
A | TRP195 |
A | ARG205 |
B | ARG73 |
B | ILE74 |
B | VAL75 |
B | VAL76 |
B | SER88 |
B | THR89 |
B | SER93 |
B | GLN94 |
B | LYS95 |
B | GLN152 |
B | SER153 |
B | HOH305 |
B | HOH410 |
B | HOH446 |
B | HOH452 |
B | HOH465 |
B | HOH495 |
B | HOH609 |
Functional Information from PROSITE/UniProt
site_id | PS01064 |
Number of Residues | 14 |
Details | PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. LEFWGngqeRLHER |
Chain | Residue | Details |
A | LEU192-ARG205 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23897464, ECO:0007744|PDB:4HMT, ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV |
Chain | Residue | Details |
A | SER18 | |
A | ARG139 | |
B | SER18 | |
B | ARG139 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15502343, ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9, ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT, ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV |
Chain | Residue | Details |
A | ARG73 | |
B | GLN117 | |
B | GLN152 | |
B | ARG205 | |
A | SER88 | |
A | GLN94 | |
A | GLN117 | |
A | GLN152 | |
A | ARG205 | |
B | ARG73 | |
B | SER88 | |
B | GLN94 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23897464, ECO:0007744|PDB:4HMT |
Chain | Residue | Details |
A | HIS90 | |
A | SER147 | |
B | HIS90 | |
B | SER147 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g79 |
Chain | Residue | Details |
A | ARG201 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g79 |
Chain | Residue | Details |
B | ARG201 |