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 |