1TDT
THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINYLTRANSFERASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008666 | molecular_function | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity |
| A | 0009085 | biological_process | L-lysine biosynthetic process |
| A | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008666 | molecular_function | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity |
| B | 0009085 | biological_process | L-lysine biosynthetic process |
| B | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008666 | molecular_function | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity |
| C | 0009085 | biological_process | L-lysine biosynthetic process |
| C | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00101 |
| Number of Residues | 29 |
| Details | HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VDegTmVdtwAtVGscAqIGknVhLsggV |
| Chain | Residue | Details |
| A | VAL134-VAL162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2tdt |
| Chain | Residue | Details |
| A | GLY166 | |
| A | GLU169 | |
| A | ASP141 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2tdt |
| Chain | Residue | Details |
| B | GLY166 | |
| B | GLU169 | |
| B | ASP141 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2tdt |
| Chain | Residue | Details |
| C | GLY166 | |
| C | GLU169 | |
| C | ASP141 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 932 |
| Chain | Residue | Details |
| A | ASP141 | covalent catalysis |
| A | GLY166 | electrostatic stabiliser |
| A | GLU189 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 932 |
| Chain | Residue | Details |
| B | ASP141 | covalent catalysis |
| B | GLY166 | electrostatic stabiliser |
| B | GLU189 | proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 932 |
| Chain | Residue | Details |
| C | ASP141 | covalent catalysis |
| C | GLY166 | electrostatic stabiliser |
| C | GLU189 | proton shuttle (general acid/base) |
