3PUL
Crystal structure of the complex of Dhydrodipicolinate synthase from Acinetobacter baumannii with lysine at 2.3A 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 | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 292 |
Chain | Residue |
A | ILE250 |
A | LYS253 |
A | TRP254 |
A | HIS257 |
A | ASP263 |
A | THR264 |
A | ILE266 |
A | PRO272 |
A | LEU273 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 293 |
Chain | Residue |
A | VAL135 |
A | ARG138 |
A | PHE244 |
A | HOH313 |
A | HOH346 |
A | HOH385 |
A | HOH418 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 294 |
Chain | Residue |
A | ASN80 |
A | TYR106 |
A | HOH311 |
A | HOH405 |
B | ASN80 |
B | TYR106 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE LYS B 292 |
Chain | Residue |
A | LYS109 |
B | VAL135 |
B | ARG138 |
B | PHE244 |
B | GLU246 |
B | SER247 |
B | ASN248 |
B | HOH341 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 293 |
Chain | Residue |
A | THR50 |
A | LEU51 |
A | SER52 |
B | SER81 |
B | GLU84 |
B | GLU87 |
B | HOH410 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 294 |
Chain | Residue |
B | GLU189 |
B | ASN233 |
B | ALA237 |
B | HIS240 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 295 |
Chain | Residue |
B | LYS224 |
B | ASP225 |
B | GLU226 |
B | GLN227 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 296 |
Chain | Residue |
A | ASN108 |
B | THR44 |
B | GLU47 |
B | ALA48 |
B | SER49 |
B | ARG138 |
B | ASN248 |
B | PRO249 |
B | LEU270 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 297 |
Chain | Residue |
B | ALA8 |
B | GLY43 |
B | THR44 |
B | THR45 |
B | LEU101 |
B | TYR133 |
B | LYS161 |
B | ILE203 |
Functional Information from PROSITE/UniProt