1R0K
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase from Zymomonas mobilis
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 | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
A | 0046872 | molecular_function | metal ion binding |
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 | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0070402 | molecular_function | NADPH binding |
C | 0008299 | biological_process | isoprenoid biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
C | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0070402 | molecular_function | NADPH binding |
D | 0008299 | biological_process | isoprenoid biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
D | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 1301 |
Chain | Residue |
A | THR13 |
A | ASN39 |
A | ARG40 |
A | ASN41 |
A | HOH1356 |
A | HOH1493 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 1302 |
Chain | Residue |
B | ARG40 |
B | ASN41 |
B | THR13 |
B | ALA38 |
B | ASN39 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT C 1303 |
Chain | Residue |
C | THR13 |
C | ASN39 |
C | ARG40 |
C | ASN41 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT D 1304 |
Chain | Residue |
D | THR13 |
D | ASN39 |
D | ARG40 |
D | ASN41 |
D | HOH1306 |
D | HOH1544 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 76 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00183 |
Chain | Residue | Details |
A | THR13 | |
A | ASP150 | |
A | SER151 | |
A | GLU152 | |
A | SER176 | |
A | HIS199 | |
A | GLY205 | |
A | SER212 | |
A | ASN217 | |
A | LYS218 | |
A | GLU221 | |
A | GLY14 | |
B | THR13 | |
B | GLY14 | |
B | SER15 | |
B | ILE16 | |
B | ARG40 | |
B | ASN41 | |
B | ASN124 | |
B | LYS125 | |
B | GLU126 | |
B | ASP150 | |
A | SER15 | |
B | SER151 | |
B | GLU152 | |
B | SER176 | |
B | HIS199 | |
B | GLY205 | |
B | SER212 | |
B | ASN217 | |
B | LYS218 | |
B | GLU221 | |
C | THR13 | |
A | ILE16 | |
C | GLY14 | |
C | SER15 | |
C | ILE16 | |
C | ARG40 | |
C | ASN41 | |
C | ASN124 | |
C | LYS125 | |
C | GLU126 | |
C | ASP150 | |
C | SER151 | |
A | ARG40 | |
C | GLU152 | |
C | SER176 | |
C | HIS199 | |
C | GLY205 | |
C | SER212 | |
C | ASN217 | |
C | LYS218 | |
C | GLU221 | |
D | THR13 | |
D | GLY14 | |
A | ASN41 | |
D | SER15 | |
D | ILE16 | |
D | ARG40 | |
D | ASN41 | |
D | ASN124 | |
D | LYS125 | |
D | GLU126 | |
D | ASP150 | |
D | SER151 | |
D | GLU152 | |
A | ASN124 | |
D | SER176 | |
D | HIS199 | |
D | GLY205 | |
D | SER212 | |
D | ASN217 | |
D | LYS218 | |
D | GLU221 | |
A | LYS125 | |
A | GLU126 |