3ANM
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) complexed with 5-phenylpyridin-2-ylmethylphosphonic acid
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 | 13 |
| Details | BINDING SITE FOR RESIDUE SYD A 800 |
| Chain | Residue |
| A | GLY184 |
| A | HOH415 |
| A | HOH419 |
| A | HOH451 |
| A | HOH463 |
| A | SER185 |
| A | HIS208 |
| A | ASN210 |
| A | TRP211 |
| A | SER221 |
| A | ASN226 |
| A | LYS227 |
| A | SER253 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NDP A 410 |
| Chain | Residue |
| A | GLY7 |
| A | THR9 |
| A | GLY10 |
| A | SER11 |
| A | ILE12 |
| A | ALA34 |
| A | GLY35 |
| A | LYS36 |
| A | ASN37 |
| A | ASP56 |
| A | ALA99 |
| A | ILE100 |
| A | VAL101 |
| A | ALA104 |
| A | ALA122 |
| A | ASN123 |
| A | LYS124 |
| A | ASP149 |
| A | MET275 |
| A | HOH443 |
| A | HOH447 |
| A | HOH475 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SYD B 801 |
| Chain | Residue |
| B | GLU151 |
| B | GLY184 |
| B | SER185 |
| B | HIS208 |
| B | ASN210 |
| B | TRP211 |
| B | MET213 |
| B | SER221 |
| B | ASN226 |
| B | LYS227 |
| B | SER253 |
| B | HOH414 |
| B | HOH445 |
| B | HOH473 |
| B | HOH585 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP B 410 |
| Chain | Residue |
| B | GLY7 |
| B | THR9 |
| B | GLY10 |
| B | SER11 |
| B | ILE12 |
| B | ALA34 |
| B | GLY35 |
| B | LYS36 |
| B | ASN37 |
| B | ASP56 |
| B | ALA99 |
| B | ILE100 |
| B | VAL101 |
| B | ALA104 |
| B | ALA122 |
| B | ASN123 |
| B | LYS124 |
| B | ASP149 |
| B | MET275 |
| B | HOH413 |
| B | HOH435 |
| B | HOH450 |
| B | HOH594 |
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 |
