1T1S
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 | 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 | obsolete isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| A | 0070402 | molecular_function | NADPH 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 | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051484 | biological_process | obsolete 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
| Chain | Residue |
| A | GLY184 |
| A | SER185 |
| A | HIS208 |
| A | SER221 |
| A | LYS227 |
| A | CBQ2001 |
| A | HOH2051 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
| Chain | Residue |
| B | HIS208 |
| B | TRP211 |
| B | SER221 |
| B | ASN226 |
| B | LYS227 |
| B | CBQ3001 |
| B | HOH3046 |
| B | GLY184 |
| B | SER185 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1002 |
| Chain | Residue |
| A | LYS124 |
| A | ASP149 |
| A | GLU151 |
| A | GLU230 |
| A | CBQ2001 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CBQ A 2001 |
| Chain | Residue |
| A | LYS124 |
| A | ASP149 |
| A | SER150 |
| A | GLU151 |
| A | TRP211 |
| A | MET213 |
| A | ILE217 |
| A | ASN226 |
| A | GLU230 |
| A | HIS256 |
| A | PRO273 |
| A | SO41001 |
| A | MG1002 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CBQ B 3001 |
| Chain | Residue |
| B | LYS124 |
| B | ASP149 |
| B | SER150 |
| B | GLU151 |
| B | TRP211 |
| B | MET213 |
| B | ASN226 |
| B | GLU230 |
| B | HIS256 |
| B | PRO273 |
| B | SO41002 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15567415","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q0Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12621040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ONO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ONP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
