5O5C
The crystal structure of DfoJ, the desferrioxamine biosynthetic pathway lysine decarboxylase from the fire blight disease pathogen Erwinia amylovora
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016830 | molecular_function | carbon-carbon lyase activity |
| E | 0016831 | molecular_function | carboxy-lyase activity |
| E | 0019752 | biological_process | carboxylic acid metabolic process |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016830 | molecular_function | carbon-carbon lyase activity |
| F | 0016831 | molecular_function | carboxy-lyase activity |
| F | 0019752 | biological_process | carboxylic acid metabolic process |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue PLP A 601 |
| Chain | Residue |
| A | LEU108 |
| A | HIS327 |
| A | LYS328 |
| A | HOH711 |
| B | THR377 |
| B | THR378 |
| A | GLY168 |
| A | THR169 |
| A | HIS214 |
| A | GLY269 |
| A | THR271 |
| A | ASP296 |
| A | ALA298 |
| A | ASP325 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue PLP B 601 |
| Chain | Residue |
| A | THR377 |
| A | THR378 |
| A | HOH715 |
| B | LEU108 |
| B | GLY168 |
| B | THR169 |
| B | ASN172 |
| B | HIS214 |
| B | GLY269 |
| B | THR271 |
| B | ASP296 |
| B | ALA298 |
| B | ASP325 |
| B | HIS327 |
| B | LYS328 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue PLP D 601 |
| Chain | Residue |
| C | THR378 |
| D | GLY167 |
| D | GLY168 |
| D | THR169 |
| D | ASN172 |
| D | HIS214 |
| D | GLY269 |
| D | THR271 |
| D | ASP296 |
| D | ALA298 |
| D | ASP325 |
| D | HIS327 |
| D | LYS328 |
| D | HOH704 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide PLP C 601 and LYS C 328 |
| Chain | Residue |
| C | LEU108 |
| C | CYS110 |
| C | GLY167 |
| C | GLY168 |
| C | THR169 |
| C | HIS214 |
| C | GLY269 |
| C | THR271 |
| C | ASP296 |
| C | ALA298 |
| C | ASP325 |
| C | TYR326 |
| C | HIS327 |
| C | SER329 |
| C | LEU483 |
| C | HOH709 |
| D | THR378 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide PLP E 601 and LYS E 328 |
| Chain | Residue |
| E | LEU108 |
| E | CYS110 |
| E | GLY168 |
| E | THR169 |
| E | HIS214 |
| E | GLY269 |
| E | THR271 |
| E | ASP296 |
| E | ALA298 |
| E | ASP325 |
| E | TYR326 |
| E | HIS327 |
| E | SER329 |
| F | THR377 |
| F | THR378 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide PLP F 601 and LYS F 328 |
| Chain | Residue |
| E | THR377 |
| E | THR378 |
| E | HOH707 |
| F | LEU108 |
| F | CYS110 |
| F | GLY167 |
| F | GLY168 |
| F | THR169 |
| F | ASN172 |
| F | HIS214 |
| F | GLY269 |
| F | THR271 |
| F | ASP296 |
| F | ALA298 |
| F | ASP325 |
| F | TYR326 |
| F | HIS327 |
| F | SER329 |
| F | LEU483 |
