4ZN6
X-ray Crystal Structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (IspC) from Acinetobacter baumannii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016114 | biological_process | terpenoid 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 | 0051484 | biological_process | 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 | 0016114 | biological_process | terpenoid 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 | 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 | 10 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ALA193 |
| A | HOH848 |
| A | SER194 |
| A | SER230 |
| A | ASN235 |
| A | LYS236 |
| A | HOH628 |
| A | HOH632 |
| A | HOH668 |
| A | HOH748 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | LYS124 |
| A | HIS151 |
| A | HIS208 |
| A | HOH667 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | LEU131 |
| A | ASN133 |
| A | PRO157 |
| A | VAL158 |
| A | ASP159 |
| A | HIS162 |
| A | GLU242 |
| A | HOH663 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | ALA193 |
| B | SER194 |
| B | SER230 |
| B | ASN235 |
| B | LYS236 |
| B | HOH624 |
| B | HOH652 |
| B | HOH700 |
| B | HOH752 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| A | LEU190 |
| B | LEU305 |
| B | ASP306 |
| B | LEU307 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00183 |
| Chain | Residue | Details |
| A | ASN235 | |
| A | LYS236 | |
| A | GLU239 | |
| B | THR19 | |
| B | GLY20 | |
| B | SER21 | |
| B | ILE22 | |
| B | ASN133 | |
| B | LYS134 | |
| B | GLU135 | |
| B | ASP159 | |
| B | SER160 | |
| B | GLU161 | |
| B | SER194 | |
| B | HIS217 | |
| B | GLY223 | |
| B | SER230 | |
| B | ASN235 | |
| B | LYS236 | |
| B | GLU239 | |
| A | GLY20 | |
| A | SER21 | |
| A | ILE22 | |
| A | ASN133 | |
| A | LYS134 | |
| A | GLU135 | |
| A | ASP159 | |
| A | SER160 | |
| A | GLU161 | |
| A | SER194 | |
| A | HIS217 | |
| A | GLY223 | |
| A | SER230 | |
| A | THR19 |
