3RK8
Crystal structure of the chloride inhibited dihydrodipicolinate synthase from Acinetobacter baumannii complexed with pyruvate at 1.8 A 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 | 10 |
Details | BINDING SITE FOR RESIDUE PYR A 292 |
Chain | Residue |
A | TYR133 |
A | HOH594 |
A | VAL135 |
A | ARG138 |
A | LYS161 |
A | GLY186 |
A | VAL205 |
A | ASN248 |
A | HOH415 |
A | HOH419 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 293 |
Chain | Residue |
A | LYS15 |
A | THR264 |
A | GLY265 |
A | ILE266 |
A | PRO272 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 294 |
Chain | Residue |
A | GLN3 |
A | GLY4 |
A | ASN37 |
A | ALA219 |
A | ILE222 |
A | HOH352 |
A | HOH447 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 295 |
Chain | Residue |
A | ASP20 |
A | TRP21 |
A | LYS22 |
A | HOH424 |
A | HOH438 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 296 |
Chain | Residue |
A | GLU54 |
A | GLU55 |
A | GLN58 |
A | HOH436 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 297 |
Chain | Residue |
A | GLU25 |
A | ARG65 |
A | HOH420 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 298 |
Chain | Residue |
A | ASP16 |
A | ARG267 |
A | HOH404 |
A | HOH443 |
A | HOH445 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 299 |
Chain | Residue |
A | THR44 |
A | LEU101 |
A | LYS161 |
A | HOH403 |
A | HOH417 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PYR B 292 |
Chain | Residue |
B | TYR133 |
B | VAL135 |
B | ARG138 |
B | LYS161 |
B | GLY186 |
B | VAL205 |
B | ASN248 |
B | HOH425 |
B | HOH428 |
B | HOH605 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 293 |
Chain | Residue |
B | LYS15 |
B | THR264 |
B | GLY265 |
B | ILE266 |
B | PRO272 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 294 |
Chain | Residue |
B | ALA182 |
B | ASP200 |
B | GOL295 |
B | HOH377 |
B | HOH387 |
B | HOH576 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 295 |
Chain | Residue |
B | MET195 |
B | GLY198 |
B | ALA199 |
B | ILE222 |
B | LYS224 |
B | GOL294 |
B | HOH576 |
B | HOH578 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 296 |
Chain | Residue |
B | GLY165 |
B | ASP187 |
B | GLU189 |
B | HOH474 |
B | HOH557 |
B | HOH590 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG B 297 |
Chain | Residue |
B | TRP21 |
B | GLN58 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 298 |
Chain | Residue |
B | LEU101 |
B | LYS161 |
B | HOH401 |
B | HOH427 |
B | HOH599 |
Functional Information from PROSITE/UniProt