1Q0H
Crystal structure of selenomethionine-labelled DXR in complex with fosmidomycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016114 | biological_process | terpenoid 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FOM A 400 |
| Chain | Residue |
| A | SER151 |
| A | MSE276 |
| A | HOH415 |
| A | HOH464 |
| A | HOH653 |
| A | GLU152 |
| A | GLY185 |
| A | SER186 |
| A | HIS209 |
| A | SER222 |
| A | ASN227 |
| A | LYS228 |
| A | GLU231 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP A 401 |
| Chain | Residue |
| A | GLY8 |
| A | THR10 |
| A | GLY11 |
| A | SER12 |
| A | ILE13 |
| A | ALA35 |
| A | GLY36 |
| A | LYS37 |
| A | ASN38 |
| A | ASP57 |
| A | ILE101 |
| A | VAL102 |
| A | MSE214 |
| A | GLY215 |
| A | ARG216 |
| A | LYS217 |
| A | HOH413 |
| A | HOH429 |
| A | HOH559 |
| A | HOH581 |
| A | HOH587 |
| A | HOH618 |
| A | HOH647 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CIT A 402 |
| Chain | Residue |
| A | CYS15 |
| A | ARG41 |
| A | ARG352 |
| A | ALA397 |
| A | SER398 |
| A | HOH483 |
| A | HOH629 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 17 |
| 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 | |
| A | GLY11 | |
| A | SER12 | |
| A | ILE13 | |
| A | GLY36 | |
| A | LYS37 | |
| A | ASN38 | |
| A | ASN124 | |
| A | LYS125 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12621040, ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP |
| Chain | Residue | Details |
| A | ASP150 | |
| A | GLU152 | |
| A | GLU231 |
