1Q0Q
Crystal structure of DXR in complex with the substrate 1-deoxy-D-xylulose-5-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| A | 0070402 | molecular_function | NADPH binding |
| A | 1990065 | cellular_component | Dxr protein complex |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| B | 0070402 | molecular_function | NADPH binding |
| B | 1990065 | cellular_component | Dxr protein complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DXP A 701 |
| Chain | Residue |
| A | LYS125 |
| A | ASN227 |
| A | LYS228 |
| A | GLU231 |
| A | MET276 |
| A | NDP2001 |
| A | HOH2093 |
| A | HOH2094 |
| A | HOH2110 |
| A | ASP150 |
| A | SER151 |
| A | GLU152 |
| A | SER186 |
| A | HIS209 |
| A | TRP212 |
| A | ILE218 |
| A | SER222 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DXP B 702 |
| Chain | Residue |
| B | LYS125 |
| B | ASP150 |
| B | SER151 |
| B | GLU152 |
| B | SER186 |
| B | HIS209 |
| B | TRP212 |
| B | ILE218 |
| B | SER222 |
| B | ASN227 |
| B | LYS228 |
| B | GLU231 |
| B | NDP2002 |
| B | HOH2131 |
| B | HOH2132 |
| B | HOH2251 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP A 2001 |
| Chain | Residue |
| A | GLY8 |
| A | THR10 |
| A | GLY11 |
| A | SER12 |
| A | ILE13 |
| A | ALA35 |
| A | GLY36 |
| A | LYS37 |
| A | ASN38 |
| A | ASP57 |
| A | ALA100 |
| A | ILE101 |
| A | VAL102 |
| A | ALA123 |
| A | ASN124 |
| A | LYS125 |
| A | GLU126 |
| A | ASP150 |
| A | MET214 |
| A | GLY215 |
| A | ILE218 |
| A | MET276 |
| A | DXP701 |
| A | HOH2003 |
| A | HOH2004 |
| A | HOH2009 |
| A | HOH2018 |
| A | HOH2019 |
| A | HOH2022 |
| A | HOH2035 |
| A | HOH2067 |
| A | HOH2114 |
| A | HOH2187 |
| A | HOH2190 |
| A | HOH2191 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NDP B 2002 |
| Chain | Residue |
| B | HOH2075 |
| B | HOH2096 |
| B | HOH2159 |
| B | HOH2270 |
| B | HOH2273 |
| B | GLY8 |
| B | THR10 |
| B | GLY11 |
| B | SER12 |
| B | ILE13 |
| B | ALA35 |
| B | GLY36 |
| B | LYS37 |
| B | ASN38 |
| B | ASP57 |
| B | ALA100 |
| B | ILE101 |
| B | VAL102 |
| B | ALA105 |
| B | ALA123 |
| B | ASN124 |
| B | LYS125 |
| B | GLU126 |
| B | ASP150 |
| B | MET214 |
| B | GLY215 |
| B | ILE218 |
| B | MET276 |
| B | DXP702 |
| B | HOH2043 |
| B | HOH2044 |
| B | HOH2045 |
| B | HOH2046 |
| B | HOH2050 |
| B | HOH2063 |
| B | HOH2065 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15567415, ECO:0007744|PDB:1Q0Q |
| Chain | Residue | Details |
| A | THR10 | |
| A | GLU126 | |
| A | SER151 | |
| A | SER186 | |
| A | HIS209 | |
| A | GLY215 | |
| A | SER222 | |
| A | ASN227 | |
| A | LYS228 | |
| B | THR10 | |
| B | GLY11 | |
| A | GLY11 | |
| B | SER12 | |
| B | ILE13 | |
| B | GLY36 | |
| B | LYS37 | |
| B | ASN38 | |
| B | ASN124 | |
| B | LYS125 | |
| B | GLU126 | |
| B | SER151 | |
| B | SER186 | |
| A | SER12 | |
| B | HIS209 | |
| B | GLY215 | |
| B | SER222 | |
| B | ASN227 | |
| B | LYS228 | |
| A | ILE13 | |
| A | GLY36 | |
| A | LYS37 | |
| A | ASN38 | |
| A | ASN124 | |
| A | LYS125 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12621040, ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP |
| Chain | Residue | Details |
| A | ASP150 | |
| A | GLU152 | |
| A | GLU231 | |
| B | ASP150 | |
| B | GLU152 | |
| B | GLU231 |
