1T1R
Crystal Structure of the Reductoisomerase Complexed with a Bisphosphonate
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 |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016114 | biological_process | terpenoid 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
| Chain | Residue |
| A | GLY184 |
| A | SER185 |
| A | HIS208 |
| A | SER221 |
| A | ASN226 |
| A | LYS227 |
| A | IMB3001 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
| Chain | Residue |
| B | HIS208 |
| B | SER221 |
| B | ASN226 |
| B | LYS227 |
| B | IMB2001 |
| B | GLY184 |
| B | SER185 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE IMB B 2001 |
| Chain | Residue |
| B | LYS124 |
| B | ASP149 |
| B | SER150 |
| B | GLU151 |
| B | TRP211 |
| B | MET213 |
| B | ASN226 |
| B | LYS227 |
| B | GLU230 |
| B | PRO273 |
| B | MET275 |
| B | SO41002 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IMB A 3001 |
| Chain | Residue |
| A | LYS124 |
| A | ASP149 |
| A | SER150 |
| A | GLU151 |
| A | TRP211 |
| A | MET213 |
| A | ASN226 |
| A | GLU230 |
| A | PRO273 |
| A | MET275 |
| A | SO41001 |
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 | THR9 | |
| A | GLU125 | |
| A | SER150 | |
| A | SER185 | |
| A | HIS208 | |
| A | GLY214 | |
| A | SER221 | |
| A | ASN226 | |
| A | LYS227 | |
| B | THR9 | |
| B | GLY10 | |
| A | GLY10 | |
| B | SER11 | |
| B | ILE12 | |
| B | GLY35 | |
| B | LYS36 | |
| B | ASN37 | |
| B | ASN123 | |
| B | LYS124 | |
| B | GLU125 | |
| B | SER150 | |
| B | SER185 | |
| A | SER11 | |
| B | HIS208 | |
| B | GLY214 | |
| B | SER221 | |
| B | ASN226 | |
| B | LYS227 | |
| A | ILE12 | |
| A | GLY35 | |
| A | LYS36 | |
| A | ASN37 | |
| A | ASN123 | |
| A | LYS124 |
| 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 | ASP149 | |
| A | GLU151 | |
| A | GLU230 | |
| B | ASP149 | |
| B | GLU151 | |
| B | GLU230 |
