6OUV
1-deoxy-D-xylulose 5-phosphate synthase (DXPS) from Deinococcus radiodurans with methylacetylphosphonate (MAP) bound
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 PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue TDK A 701 |
| Chain | Residue |
| A | HIS51 |
| A | GLY155 |
| A | SER156 |
| A | ASN183 |
| A | MET185 |
| A | SER186 |
| A | ILE187 |
| A | LYS289 |
| A | HIS304 |
| A | MET349 |
| A | ILE371 |
| A | SER54 |
| A | GLU373 |
| A | PHE398 |
| A | ARG401 |
| A | ASP430 |
| A | HIS434 |
| A | MG702 |
| A | HOH803 |
| A | HOH828 |
| A | HOH863 |
| A | HOH919 |
| A | VAL80 |
| A | HOH963 |
| A | HOH1028 |
| A | HIS82 |
| A | GLY123 |
| A | HIS124 |
| A | ALA125 |
| A | GLY153 |
| A | ASP154 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 702 |
| Chain | Residue |
| A | ASP154 |
| A | ASN183 |
| A | MET185 |
| A | TDK701 |
| A | HOH828 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 703 |
| Chain | Residue |
| A | ASN416 |
| A | ALA467 |
| A | HIS470 |
| A | GLY472 |
| A | HOH887 |
| A | HOH975 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue TDK B 701 |
| Chain | Residue |
| B | HIS51 |
| B | SER54 |
| B | VAL80 |
| B | HIS82 |
| B | GLY123 |
| B | HIS124 |
| B | ALA125 |
| B | GLY153 |
| B | ASP154 |
| B | GLY155 |
| B | SER156 |
| B | ASN183 |
| B | MET185 |
| B | SER186 |
| B | ILE187 |
| B | LYS289 |
| B | HIS304 |
| B | MET349 |
| B | ILE371 |
| B | GLU373 |
| B | PHE398 |
| B | ARG401 |
| B | ASP430 |
| B | HIS434 |
| B | MG702 |
| B | HOH809 |
| B | HOH820 |
| B | HOH838 |
| B | HOH859 |
| B | HOH880 |
| B | HOH947 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 702 |
| Chain | Residue |
| B | ASP154 |
| B | ASN183 |
| B | MET185 |
| B | TDK701 |
| B | HOH838 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 703 |
| Chain | Residue |
| B | ASN416 |
| B | ALA467 |
| B | HIS470 |
| B | GLY472 |
| B | HOH920 |
| B | HOH980 |
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 |
