4HMV
Crystal structure of PhzG from Pseudomonas fluorescens 2-79 in complex with tetrahydrophenazine-1-carboxylic acid after 5 days of soaking
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 | 23 |
Details | BINDING SITE FOR RESIDUE FMN A 301 |
Chain | Residue |
A | ARG73 |
A | GLN152 |
A | SER153 |
A | WUB303 |
A | HOH406 |
A | HOH411 |
A | HOH423 |
A | HOH455 |
A | HOH459 |
B | LEU19 |
B | TYR110 |
A | ILE74 |
B | GLN117 |
B | TRP195 |
B | ARG205 |
B | HOH422 |
A | VAL75 |
A | VAL76 |
A | SER88 |
A | THR89 |
A | SER93 |
A | GLN94 |
A | LYS95 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | GLN67 |
A | ARG69 |
A | ARG188 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE WUB A 303 |
Chain | Residue |
A | VAL76 |
A | SER88 |
A | ARG139 |
A | TYR182 |
A | FMN301 |
A | HOH572 |
B | SER18 |
B | LEU19 |
B | HOH602 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE FMN B 301 |
Chain | Residue |
A | TYR110 |
A | GLN117 |
A | TRP195 |
A | ARG205 |
A | HOH413 |
B | ARG73 |
B | ILE74 |
B | VAL75 |
B | VAL76 |
B | SER88 |
B | THR89 |
B | SER93 |
B | GLN94 |
B | LYS95 |
B | GLN152 |
B | SER153 |
B | HOH416 |
B | HOH433 |
B | HOH435 |
B | HOH456 |
B | HOH493 |
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 |