3RAS
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) complexed with a lipophilic phosphonate inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0050897 | molecular_function | cobalt ion binding |
| A | 0051483 | biological_process | terpenoid biosynthetic process, mevalonate-independent |
| A | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0050897 | molecular_function | cobalt ion binding |
| B | 0051483 | biological_process | terpenoid biosynthetic process, mevalonate-independent |
| B | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| B | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NDP A 1391 |
| Chain | Residue |
| A | GLY19 |
| A | HIS50 |
| A | ALA69 |
| A | ALA103 |
| A | LEU104 |
| A | LEU108 |
| A | ALA126 |
| A | ASN127 |
| A | LYS128 |
| A | GLU129 |
| A | ASP151 |
| A | THR21 |
| A | MET205 |
| A | GLY206 |
| A | PRO207 |
| A | ASN209 |
| A | MET267 |
| A | FM5390 |
| A | DCV391 |
| A | HOH399 |
| A | GLY22 |
| A | SER23 |
| A | ILE24 |
| A | ALA46 |
| A | GLY47 |
| A | GLY48 |
| A | ALA49 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FM5 A 390 |
| Chain | Residue |
| A | ASP151 |
| A | SER152 |
| A | GLU153 |
| A | ALA176 |
| A | SER177 |
| A | TRP203 |
| A | MET205 |
| A | ASN209 |
| A | SER213 |
| A | ASN218 |
| A | LYS219 |
| A | GLU222 |
| A | SER245 |
| A | DCV391 |
| A | MN392 |
| A | NDP1391 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DCV A 391 |
| Chain | Residue |
| A | LYS128 |
| A | ASP151 |
| A | SER152 |
| A | ALA176 |
| A | SER177 |
| A | TRP203 |
| A | MET205 |
| A | ASN209 |
| A | SER213 |
| A | ASN218 |
| A | LYS219 |
| A | GLU222 |
| A | SER245 |
| A | FM5390 |
| A | MN392 |
| A | NDP1391 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP B 1392 |
| Chain | Residue |
| B | GLY19 |
| B | THR21 |
| B | GLY22 |
| B | SER23 |
| B | ILE24 |
| B | ALA46 |
| B | GLY47 |
| B | GLY48 |
| B | ALA49 |
| B | HIS50 |
| B | ALA69 |
| B | ALA103 |
| B | LEU104 |
| B | LEU108 |
| B | ALA126 |
| B | ASN127 |
| B | LYS128 |
| B | ASP151 |
| B | MET267 |
| B | HOH397 |
| B | HOH422 |
| B | HOH423 |
| B | HOH434 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 392 |
| Chain | Residue |
| A | ASP151 |
| A | GLU153 |
| A | GLU222 |
| A | FM5390 |
| A | DCV391 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FM5 B 390 |
| Chain | Residue |
| B | THR21 |
| B | HIS50 |
| B | THR53 |
| B | TRP203 |
| B | DCV391 |
| B | HOH412 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DCV B 391 |
| Chain | Residue |
| B | HIS50 |
| B | THR53 |
| B | TRP203 |
| B | FM5390 |
| B | HOH395 |
| B | HOH412 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 392 |
| Chain | Residue |
| B | ASP151 |
| B | GLU153 |
| B | GLU222 |
| B | HOH462 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 393 |
| Chain | Residue |
| B | ALA176 |
| B | SER177 |
| B | SER213 |
| B | ASN218 |
| B | LYS219 |
| B | HOH444 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00183 |
| Chain | Residue | Details |
| A | THR21 | |
| A | SER152 | |
| A | GLU153 | |
| A | SER177 | |
| A | HIS200 | |
| A | GLY206 | |
| A | SER213 | |
| A | ASN218 | |
| A | LYS219 | |
| A | GLU222 | |
| B | THR21 | |
| A | GLY22 | |
| B | GLY22 | |
| B | SER23 | |
| B | ILE24 | |
| B | GLY47 | |
| B | ASN127 | |
| B | LYS128 | |
| B | GLU129 | |
| B | ASP151 | |
| B | SER152 | |
| B | GLU153 | |
| A | SER23 | |
| B | SER177 | |
| B | HIS200 | |
| B | GLY206 | |
| B | SER213 | |
| B | ASN218 | |
| B | LYS219 | |
| B | GLU222 | |
| A | ILE24 | |
| A | GLY47 | |
| A | ASN127 | |
| A | LYS128 | |
| A | GLU129 | |
| A | ASP151 |
