3PUE
Crystal structure of the complex of Dhydrodipicolinate synthase from Acinetobacter baumannii with lysine at 2.6A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 292 |
| Chain | Residue |
| A | VAL135 |
| A | ARG138 |
| A | PHE244 |
| A | HOH328 |
| A | HOH335 |
| B | LYS109 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 293 |
| Chain | Residue |
| A | THR45 |
| A | LEU101 |
| A | TYR133 |
| A | LYS161 |
| A | ILE203 |
| A | HOH333 |
| A | ALA8 |
| A | GLY43 |
| A | THR44 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LYS B 292 |
| Chain | Residue |
| A | LYS109 |
| B | VAL135 |
| B | ARG138 |
| B | PHE244 |
| B | SER247 |
| B | ASN248 |
| B | HOH312 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 293 |
| Chain | Residue |
| B | ASP225 |
| B | GLU226 |
| B | GLN227 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 294 |
| Chain | Residue |
| A | THR50 |
| B | SER81 |
| B | ARG83 |
| B | GLU84 |
| B | GLU87 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 295 |
| Chain | Residue |
| B | ALA8 |
| B | VAL40 |
| B | GLY43 |
| B | THR44 |
| B | THR45 |
| B | LEU101 |
| B | TYR133 |
| B | LYS161 |
| B | ILE203 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 296 |
| Chain | Residue |
| B | LYS26 |
| B | LEU261 |
Functional Information from PROSITE/UniProt
