4HMT
Crystal structure of PhzG from Pseudomonas fluorescens 2-79 in complex with hexahydrophenazine-1,6-dicarboxylic 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 | 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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 301 |
| Chain | Residue |
| A | ARG73 |
| A | GLN152 |
| A | SER153 |
| A | NNV302 |
| A | HOH407 |
| A | HOH412 |
| A | HOH424 |
| A | HOH460 |
| B | LEU19 |
| B | TYR110 |
| B | GLN117 |
| A | ILE74 |
| 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 | 13 |
| Details | BINDING SITE FOR RESIDUE NNV A 302 |
| Chain | Residue |
| A | SER88 |
| A | HIS90 |
| A | ARG139 |
| A | SER147 |
| A | TYR182 |
| A | FMN301 |
| A | HOH530 |
| A | HOH617 |
| A | HOH619 |
| B | SER18 |
| B | HIS203 |
| B | HOH485 |
| B | HOH585 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | GLN67 |
| A | ARG69 |
| A | ARG188 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | GLN31 |
| A | ARG219 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 305 |
| Chain | Residue |
| A | ARG57 |
| A | SER78 |
| A | GLU79 |
| A | ILE80 |
| A | HOH560 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 301 |
| Chain | Residue |
| A | LEU19 |
| A | TYR110 |
| A | GLN117 |
| A | TRP195 |
| A | ARG205 |
| A | HOH414 |
| B | ARG73 |
| B | ILE74 |
| B | VAL75 |
| B | VAL76 |
| B | SER88 |
| B | THR89 |
| B | SER93 |
| B | GLN94 |
| B | LYS95 |
| B | GLN152 |
| B | SER153 |
| B | NNV302 |
| B | HOH416 |
| B | HOH432 |
| B | HOH434 |
| B | HOH453 |
| B | HOH488 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NNV B 302 |
| Chain | Residue |
| A | SER18 |
| A | LEU19 |
| A | HIS203 |
| A | HOH607 |
| A | HOH635 |
| B | SER88 |
| B | HIS90 |
| B | ARG139 |
| B | SER147 |
| B | FMN301 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| B | ARG126 |
| B | ASN129 |
| B | ARG178 |
| B | GLU180 |
| B | GLY181 |
| 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 site: {"evidences":[{"source":"PubMed","id":"23897464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HMU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HMV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15502343","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23897464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TY9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HMU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HMV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23897464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
