4HMX
Crystal structure of PhzG from Burkholderia lata 383 in complex with tetrahydrophenazine-1-carboxylic acid
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 | 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 | 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 | 21 |
| Details | BINDING SITE FOR RESIDUE FMN A 301 |
| Chain | Residue |
| A | GLU45 |
| A | LYS85 |
| A | GLN142 |
| A | SER143 |
| A | HOH401 |
| A | HOH408 |
| A | HOH525 |
| B | TYR100 |
| B | GLN107 |
| B | TRP185 |
| B | ARG195 |
| A | ARG63 |
| B | HOH402 |
| B | HOH403 |
| A | VAL64 |
| A | ILE65 |
| A | ALA66 |
| A | CYS78 |
| A | THR79 |
| A | SER83 |
| A | ARG84 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE WUB A 302 |
| Chain | Residue |
| A | HIS193 |
| A | HOH490 |
| B | CYS78 |
| B | ARG129 |
| B | GLN142 |
| B | FMN301 |
| B | HOH617 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 301 |
| Chain | Residue |
| A | TYR100 |
| A | GLN107 |
| A | TRP185 |
| A | ARG195 |
| A | WUB302 |
| A | HOH405 |
| A | HOH412 |
| B | GLU45 |
| B | ARG63 |
| B | VAL64 |
| B | ILE65 |
| B | ALA66 |
| B | CYS78 |
| B | THR79 |
| B | SER83 |
| B | ARG84 |
| B | LYS85 |
| B | GLN142 |
| B | SER143 |
| B | HOH414 |
| B | HOH422 |
| B | HOH571 |
| B | HOH576 |
| B | HOH617 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q51793 |
| Chain | Residue | Details |
| A | SER8 | |
| A | HIS80 | |
| A | ARG129 | |
| A | SER137 | |
| B | SER8 | |
| B | HIS80 | |
| B | ARG129 | |
| B | SER137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23897464, ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX |
| Chain | Residue | Details |
| A | ARG63 | |
| B | GLN107 | |
| B | GLN142 | |
| B | ARG195 | |
| A | CYS78 | |
| A | ARG84 | |
| A | GLN107 | |
| A | GLN142 | |
| A | ARG195 | |
| B | ARG63 | |
| B | CYS78 | |
| B | ARG84 |
