8V9I
1-deoxy-D-xylulose 5-phosphate synthase (DXPS) from Deinococcus radiodurans with D-phenylalanine-derived triazole acetylphosphonate (D-PheTrAP) bound
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0008661 | molecular_function | 1-deoxy-D-xylulose-5-phosphate synthase activity |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052865 | biological_process | obsolete 1-deoxy-D-xylulose 5-phosphate biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0008661 | molecular_function | 1-deoxy-D-xylulose-5-phosphate synthase activity |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052865 | biological_process | obsolete 1-deoxy-D-xylulose 5-phosphate biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00802 |
| Number of Residues | 17 |
| Details | TRANSKETOLASE_2 Transketolase signature 2. GADGATHnGVFdlSflR |
| Chain | Residue | Details |
| A | GLY428-ARG444 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17135236","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 333 |
| Chain | Residue | Details |
| A | LYS289 | electrostatic stabiliser |
| A | GLU373 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG401 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 333 |
| Chain | Residue | Details |
| B | LYS289 | electrostatic stabiliser |
| B | GLU373 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG401 | electrostatic stabiliser, hydrogen bond donor |
