4OOE
M. tuberculosis 1-deoxy-d-xylulose-5-phosphate reductoisomerase W203Y mutant bound to fosmidomycin and NADPH
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 |
| C | 0000287 | molecular_function | magnesium ion 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 | 0030145 | molecular_function | manganese ion binding |
| C | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050897 | molecular_function | cobalt ion binding |
| C | 0051483 | biological_process | terpenoid biosynthetic process, mevalonate-independent |
| C | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0000287 | molecular_function | magnesium ion 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 | 0030145 | molecular_function | manganese ion binding |
| D | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050897 | molecular_function | cobalt ion binding |
| D | 0051483 | biological_process | terpenoid biosynthetic process, mevalonate-independent |
| D | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FOM A 500 |
| Chain | Residue |
| A | ASP151 |
| A | ASN218 |
| A | LYS219 |
| A | GLU222 |
| A | MN501 |
| A | NDP502 |
| A | HOH610 |
| A | HOH612 |
| A | HOH614 |
| A | SER152 |
| A | GLU153 |
| A | ALA176 |
| A | SER177 |
| A | HIS200 |
| A | TYR203 |
| A | MET205 |
| A | SER213 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 501 |
| Chain | Residue |
| A | ASP151 |
| A | GLU153 |
| A | GLU222 |
| A | FOM500 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NDP A 502 |
| Chain | Residue |
| A | GLY19 |
| A | THR21 |
| A | GLY22 |
| A | SER23 |
| A | ILE24 |
| A | ALA46 |
| A | GLY47 |
| A | GLY48 |
| A | ALA49 |
| A | HIS50 |
| A | ALA69 |
| A | ALA103 |
| A | LEU104 |
| A | VAL105 |
| A | LEU108 |
| A | ALA126 |
| A | ASN127 |
| A | LYS128 |
| A | GLU129 |
| A | ASP151 |
| A | MET205 |
| A | GLY206 |
| A | ASN209 |
| A | MET267 |
| A | FOM500 |
| A | HOH603 |
| A | HOH622 |
| A | HOH632 |
| A | HOH634 |
| A | HOH636 |
| A | HOH637 |
| A | HOH643 |
| A | HOH661 |
| A | HOH665 |
| A | HOH697 |
| A | HOH710 |
| A | HOH742 |
| A | HOH755 |
| A | HOH793 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FOM B 500 |
| Chain | Residue |
| B | ASP151 |
| B | SER152 |
| B | GLU153 |
| B | ALA176 |
| B | SER177 |
| B | HIS200 |
| B | TYR203 |
| B | MET205 |
| B | SER213 |
| B | ASN218 |
| B | LYS219 |
| B | GLU222 |
| B | MN501 |
| B | NDP502 |
| B | HOH602 |
| B | HOH628 |
| B | HOH634 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 501 |
| Chain | Residue |
| B | ASP151 |
| B | GLU153 |
| B | GLU222 |
| B | FOM500 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NDP B 502 |
| Chain | Residue |
| B | MET205 |
| B | GLY206 |
| B | ASN209 |
| B | MET267 |
| B | FOM500 |
| B | HOH610 |
| B | HOH630 |
| B | HOH632 |
| B | HOH636 |
| B | HOH643 |
| B | HOH654 |
| B | HOH673 |
| B | HOH742 |
| B | HOH779 |
| B | HOH823 |
| B | HOH840 |
| B | HOH872 |
| B | HOH927 |
| B | GLY19 |
| B | THR21 |
| B | GLY22 |
| B | SER23 |
| B | ILE24 |
| B | ALA46 |
| B | GLY47 |
| B | GLY48 |
| B | ALA49 |
| B | HIS50 |
| B | ALA69 |
| B | ALA103 |
| B | LEU104 |
| B | ALA126 |
| B | ASN127 |
| B | LYS128 |
| B | GLU129 |
| B | ASP151 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FOM C 500 |
| Chain | Residue |
| C | ASP151 |
| C | SER152 |
| C | GLU153 |
| C | ALA176 |
| C | SER177 |
| C | HIS200 |
| C | TYR203 |
| C | SER213 |
| C | ASN218 |
| C | LYS219 |
| C | GLU222 |
| C | MET267 |
| C | MN501 |
| C | NDP502 |
| C | HOH603 |
| C | HOH615 |
| C | HOH631 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 501 |
| Chain | Residue |
| C | LYS128 |
| C | ASP151 |
| C | GLU153 |
| C | GLU222 |
| C | FOM500 |
| site_id | AC9 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NDP C 502 |
| Chain | Residue |
| C | GLY19 |
| C | THR21 |
| C | GLY22 |
| C | SER23 |
| C | ILE24 |
| C | ALA46 |
| C | GLY47 |
| C | GLY48 |
| C | ALA49 |
| C | HIS50 |
| C | ALA69 |
| C | ALA103 |
| C | LEU104 |
| C | LEU108 |
| C | ALA126 |
| C | ASN127 |
| C | LYS128 |
| C | GLU129 |
| C | ASP151 |
| C | MET205 |
| C | GLY206 |
| C | PRO207 |
| C | ASN209 |
| C | MET267 |
| C | FOM500 |
| C | HOH613 |
| C | HOH625 |
| C | HOH632 |
| C | HOH634 |
| C | HOH647 |
| C | HOH651 |
| C | HOH655 |
| C | HOH680 |
| C | HOH801 |
| C | HOH804 |
| C | HOH840 |
| C | HOH940 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FOM D 500 |
| Chain | Residue |
| D | LYS128 |
| D | ASP151 |
| D | SER152 |
| D | GLU153 |
| D | ALA176 |
| D | SER177 |
| D | HIS200 |
| D | TYR203 |
| D | MET205 |
| D | SER213 |
| D | ASN218 |
| D | LYS219 |
| D | GLU222 |
| D | MN501 |
| D | NDP502 |
| D | HOH610 |
| D | HOH613 |
| D | HOH636 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 501 |
| Chain | Residue |
| D | ASP151 |
| D | GLU153 |
| D | GLU222 |
| D | FOM500 |
| site_id | BC3 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NDP D 502 |
| Chain | Residue |
| D | GLY19 |
| D | THR21 |
| D | GLY22 |
| D | SER23 |
| D | ILE24 |
| D | ALA46 |
| D | GLY47 |
| D | GLY48 |
| D | ALA49 |
| D | HIS50 |
| D | ALA69 |
| D | ALA103 |
| D | LEU104 |
| D | ALA126 |
| D | ASN127 |
| D | LYS128 |
| D | GLU129 |
| D | ASP151 |
| D | MET205 |
| D | GLY206 |
| D | ASN209 |
| D | MET267 |
| D | FOM500 |
| D | HOH614 |
| D | HOH615 |
| D | HOH622 |
| D | HOH643 |
| D | HOH647 |
| D | HOH681 |
| D | HOH719 |
| D | HOH752 |
| D | HOH765 |
| D | HOH863 |
| D | HOH881 |
| D | HOH888 |
| D | HOH898 |
| D | HOH947 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| 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 | |
| C | THR21 | |
| C | GLY22 | |
| C | SER23 | |
| A | ILE24 | |
| C | ILE24 | |
| C | GLY47 | |
| C | ASN127 | |
| C | LYS128 | |
| C | GLU129 | |
| C | ASP151 | |
| C | SER152 | |
| C | GLU153 | |
| C | SER177 | |
| C | HIS200 | |
| A | GLY47 | |
| C | GLY206 | |
| C | SER213 | |
| C | ASN218 | |
| C | LYS219 | |
| C | GLU222 | |
| D | THR21 | |
| D | GLY22 | |
| D | SER23 | |
| D | ILE24 | |
| D | GLY47 | |
| A | ASN127 | |
| D | ASN127 | |
| D | LYS128 | |
| D | GLU129 | |
| D | ASP151 | |
| D | SER152 | |
| D | GLU153 | |
| D | SER177 | |
| D | HIS200 | |
| D | GLY206 | |
| D | SER213 | |
| A | LYS128 | |
| D | ASN218 | |
| D | LYS219 | |
| D | GLU222 | |
| A | GLU129 | |
| A | ASP151 |
