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 |
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 | 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: 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 |