2O1X
1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Deinococcus radiodurans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0003824 | molecular_function | catalytic activity |
| 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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008299 | biological_process | isoprenoid biosynthetic process |
| C | 0008661 | molecular_function | 1-deoxy-D-xylulose-5-phosphate synthase activity |
| C | 0009228 | biological_process | thiamine biosynthetic process |
| C | 0016114 | biological_process | terpenoid biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0052865 | biological_process | 1-deoxy-D-xylulose 5-phosphate biosynthetic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0008299 | biological_process | isoprenoid biosynthetic process |
| D | 0008661 | molecular_function | 1-deoxy-D-xylulose-5-phosphate synthase activity |
| D | 0009228 | biological_process | thiamine biosynthetic process |
| D | 0016114 | biological_process | terpenoid biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0052865 | biological_process | 1-deoxy-D-xylulose 5-phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 2001 |
| Chain | Residue |
| A | ASP154 |
| A | ASN181 |
| A | ASN183 |
| A | MET185 |
| A | TPP1001 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 2002 |
| Chain | Residue |
| B | ASP154 |
| B | ASN183 |
| B | MET185 |
| B | TPP1002 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 2003 |
| Chain | Residue |
| C | ASP154 |
| C | ASN183 |
| C | MET185 |
| C | TPP1003 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 2004 |
| Chain | Residue |
| D | ASP154 |
| D | ASN183 |
| D | MET185 |
| D | TPP1004 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE TPP A 1001 |
| Chain | Residue |
| A | SER54 |
| A | HIS82 |
| A | GLY123 |
| A | HIS124 |
| A | ALA125 |
| A | GLY153 |
| A | ASP154 |
| A | GLY155 |
| A | SER156 |
| A | ASN183 |
| A | MET185 |
| A | SER186 |
| A | ILE187 |
| A | LYS289 |
| A | MET349 |
| A | ILE371 |
| A | GLU373 |
| A | PHE398 |
| A | MG2001 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TPP B 1002 |
| Chain | Residue |
| B | SER54 |
| 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 | MET349 |
| B | ILE371 |
| B | GLU373 |
| B | PHE398 |
| B | ARG401 |
| B | MG2002 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE TPP C 1003 |
| Chain | Residue |
| C | SER54 |
| C | HIS82 |
| C | GLY123 |
| C | HIS124 |
| C | ALA125 |
| C | GLY153 |
| C | ASP154 |
| C | GLY155 |
| C | SER156 |
| C | ASN183 |
| C | SER186 |
| C | ILE371 |
| C | GLU373 |
| C | PHE398 |
| C | ARG401 |
| C | MG2003 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE TPP D 1004 |
| Chain | Residue |
| D | SER54 |
| D | HIS82 |
| D | GLY123 |
| D | HIS124 |
| D | ALA125 |
| D | GLY153 |
| D | ASP154 |
| D | GLY155 |
| D | SER156 |
| D | ASN183 |
| D | MET185 |
| D | ILE187 |
| D | LYS289 |
| D | ILE371 |
| D | GLU373 |
| D | PHE398 |
| D | ARG401 |
| D | MG2004 |
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 | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17135236 |
| Chain | Residue | Details |
| A | HIS82 | |
| C | ASP154 | |
| C | ASN183 | |
| C | GLU373 | |
| D | HIS82 | |
| D | ASP154 | |
| D | ASN183 | |
| D | GLU373 | |
| A | ASP154 | |
| A | ASN183 | |
| A | GLU373 | |
| B | HIS82 | |
| B | ASP154 | |
| B | ASN183 | |
| B | GLU373 | |
| C | HIS82 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY123 | |
| A | GLY155 | |
| B | GLY123 | |
| B | GLY155 | |
| C | GLY123 | |
| C | GLY155 | |
| D | GLY123 | |
| D | GLY155 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | GLU373 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | PRO258 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | PRO258 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | PRO258 |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | VAL256 |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | VAL256 |
| site_id | CSA15 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | VAL256 |
| site_id | CSA16 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | VAL256 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | GLU373 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | GLU373 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | GLU373 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | HIS434 | |
| A | GLU373 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | HIS434 | |
| B | GLU373 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | HIS434 | |
| C | GLU373 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | HIS434 | |
| D | GLU373 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | PRO258 |
| 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 |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 333 |
| Chain | Residue | Details |
| C | LYS289 | electrostatic stabiliser |
| C | GLU373 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ARG401 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 333 |
| Chain | Residue | Details |
| D | LYS289 | electrostatic stabiliser |
| D | GLU373 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ARG401 | electrostatic stabiliser, hydrogen bond donor |
