2JD2
X-ray structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, DXR, Rv2870c, from Mycobacterium tuberculosis, in complex with manganese
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 | 6 |
Details | BINDING SITE FOR RESIDUE MN A1390 |
Chain | Residue |
A | ASP151 |
A | GLU153 |
A | GLU222 |
A | HOH2158 |
A | HOH2159 |
A | HOH2160 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A1391 |
Chain | Residue |
A | SER213 |
A | ASN218 |
A | LYS219 |
A | HOH2158 |
A | HOH2161 |
A | HOH2162 |
A | ALA176 |
A | SER177 |
A | HIS200 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A1392 |
Chain | Residue |
A | ARG162 |
A | TRP277 |
A | PRO278 |
A | HOH2163 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B1390 |
Chain | Residue |
B | ASP151 |
B | GLU153 |
B | GLU222 |
B | HOH2221 |
B | HOH2222 |
B | HOH2223 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B1391 |
Chain | Residue |
B | ALA176 |
B | SER177 |
B | SER213 |
B | ASN218 |
B | LYS219 |
B | HOH2221 |
B | HOH2224 |
B | HOH2225 |
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 |