3PUO
Crystal structure of dihydrodipicolinate synthase from Pseudomonas aeruginosa(PsDHDPS)complexed with L-lysine at 2.65A 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 |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LYS A 293 |
Chain | Residue |
A | SER48 |
A | ALA49 |
A | LEU51 |
A | ASP52 |
A | VAL53 |
A | HIS56 |
B | ASN80 |
B | GLU84 |
B | LYS293 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 294 |
Chain | Residue |
A | ARG212 |
A | ASP216 |
B | GLU124 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LYS A 295 |
Chain | Residue |
A | MET1 |
A | ILE266 |
A | ARG267 |
A | LEU268 |
A | LEU270 |
A | THR271 |
A | TRP272 |
A | HOH298 |
B | GLN117 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE LYS B 293 |
Chain | Residue |
A | GLU84 |
A | LYS293 |
B | SER48 |
B | ALA49 |
B | LEU51 |
B | GLU84 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00418 |
Chain | Residue | Details |
A | TYR133 | |
B | TYR133 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00418 |
Chain | Residue | Details |
A | LYS161 | |
B | LYS161 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418 |
Chain | Residue | Details |
A | THR45 | |
A | ILE203 | |
B | THR45 | |
B | ILE203 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Part of a proton relay during catalysis => ECO:0000255|HAMAP-Rule:MF_00418 |
Chain | Residue | Details |
A | THR44 | |
A | TYR107 | |
B | THR44 | |
B | TYR107 |