3ANN
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) complexed with quinolin-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 | 23 |
Details | BINDING SITE FOR RESIDUE NDP A 701 |
Chain | Residue |
A | GLY7 |
A | ASP56 |
A | ALA99 |
A | ILE100 |
A | VAL101 |
A | ALA104 |
A | ALA122 |
A | ASN123 |
A | LYS124 |
A | ASP149 |
A | MET275 |
A | THR9 |
A | HOH435 |
A | HOH444 |
A | HOH468 |
A | HOH485 |
A | GLY10 |
A | SER11 |
A | ILE12 |
A | ALA34 |
A | GLY35 |
A | LYS36 |
A | ASN37 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SYE A 800 |
Chain | Residue |
A | GLY184 |
A | SER185 |
A | HIS208 |
A | ASN210 |
A | TRP211 |
A | SER221 |
A | ASN226 |
A | LYS227 |
A | SER253 |
A | PRO273 |
A | HOH415 |
A | HOH428 |
A | HOH429 |
A | HOH450 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NDP B 702 |
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 | HOH428 |
B | HOH436 |
B | HOH463 |
B | HOH598 |
B | HOH603 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SYE B 801 |
Chain | Residue |
B | GLY184 |
B | SER185 |
B | HIS208 |
B | ASN210 |
B | TRP211 |
B | SER221 |
B | ASN226 |
B | LYS227 |
B | SER253 |
B | PRO273 |
B | HOH411 |
B | HOH414 |
B | HOH426 |
B | HOH429 |
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 |