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 | 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 | 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: BINDING => ECO:0000269|PubMed:17135236 |
Chain | Residue | Details |
A | HIS82 | |
A | ASP154 | |
A | ASN183 | |
A | GLU373 | |
B | HIS82 | |
B | ASP154 | |
B | ASN183 | |
B | GLU373 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY123 | |
A | GLY155 | |
B | GLY123 | |
B | GLY155 |
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 |