5T25
Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
| 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 | 0009436 | biological_process | glyoxylate catabolic process |
| 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 | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
| 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 | 0009436 | biological_process | glyoxylate catabolic process |
| 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 | 11 |
| Details | binding site for residue LYS A 301 |
| Chain | Residue |
| A | SER48 |
| B | ASN80 |
| B | GLU84 |
| A | ALA49 |
| A | LEU51 |
| A | HIS53 |
| A | HIS56 |
| A | TYR106 |
| A | HOH433 |
| A | HOH556 |
| A | HOH561 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | SER185 |
| A | ASP187 |
| A | SER190 |
| A | PHE194 |
| A | HOH518 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | THR77 |
| A | THR89 |
| A | CYS100 |
| A | ILE122 |
| A | GLN130 |
| A | HOH452 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | ALA152 |
| A | VAL154 |
| A | LYS155 |
| A | ILE157 |
| A | HOH403 |
| A | HOH611 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | ASP265 |
| A | PRO273 |
| A | ILE274 |
| A | HOH507 |
| A | HOH627 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 306 |
| Chain | Residue |
| A | ARG21 |
| A | ALA22 |
| A | HOH692 |
| A | HOH711 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue LYS B 301 |
| Chain | Residue |
| A | ASN80 |
| A | GLU84 |
| B | SER48 |
| B | ALA49 |
| B | LEU51 |
| B | HIS56 |
| B | TYR106 |
| B | HOH409 |
| B | HOH549 |
| B | HOH577 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 302 |
| Chain | Residue |
| B | ALA152 |
| B | VAL154 |
| B | LYS155 |
| B | ILE157 |
| B | HOH652 |
| B | HOH671 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 303 |
| Chain | Residue |
| B | LEU144 |
| B | PRO145 |
| B | GLU146 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 304 |
| Chain | Residue |
| B | SER111 |
| B | GLN112 |
| B | GLU113 |
| B | HOH594 |
| B | HOH683 |
| B | HOH711 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 305 |
| Chain | Residue |
| B | PRO110 |
| B | SER111 |
| B | GLN112 |
| B | HOH540 |
| B | HOH707 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue NA B 306 |
| Chain | Residue |
| B | ARG21 |
| B | ALA22 |
Functional Information from PROSITE/UniProt
| site_id | PS00665 |
| Number of Residues | 18 |
| Details | DHDPS_1 Dihydrodipicolinate synthase signature 1. AIVsvGTTGESatlnhdE |
| Chain | Residue | Details |
| A | ALA38-GLU55 |
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 | 74P161 | |
| B | 74P161 |
| 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 |
