5DNX
Crystal structure of IGPD from Pyrococcus furiosus in complex with (R)-C348
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 201 |
| Chain | Residue |
| A | HIS52 |
| A | GLU56 |
| A | GLU121 |
| A | HIS146 |
| A | 5LD203 |
| A | HOH313 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 202 |
| Chain | Residue |
| A | GLU149 |
| A | 5LD203 |
| A | HIS29 |
| A | HIS53 |
| A | HIS145 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue 5LD A 203 |
| Chain | Residue |
| A | GLU7 |
| A | HIS29 |
| A | HIS52 |
| A | HIS53 |
| A | GLU56 |
| A | MET84 |
| A | HIS145 |
| A | HIS146 |
| A | GLU149 |
| A | LYS153 |
| A | MN201 |
| A | MN202 |
| A | HOH318 |
| C | ARG76 |
| C | ARG98 |
| C | SER171 |
| C | LYS173 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 201 |
| Chain | Residue |
| B | HIS146 |
| B | 5LD201 |
| B | HOH304 |
| C | HIS52 |
| C | GLU56 |
| C | GLU121 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue 5LD B 201 |
| Chain | Residue |
| A | ARG76 |
| A | ARG98 |
| A | SER171 |
| A | LYS173 |
| B | HIS29 |
| B | MET84 |
| B | HIS145 |
| B | HIS146 |
| B | GLU149 |
| B | LYS153 |
| B | MN202 |
| B | HOH304 |
| B | HOH324 |
| C | GLU7 |
| C | HIS52 |
| C | HIS53 |
| C | GLU56 |
| C | MN201 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 202 |
| Chain | Residue |
| B | HIS29 |
| B | HIS145 |
| B | GLU149 |
| B | 5LD201 |
| C | HIS53 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 203 |
| Chain | Residue |
| B | HIS53 |
| B | 5LD205 |
| C | HIS29 |
| C | HIS145 |
| C | GLU149 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 204 |
| Chain | Residue |
| B | HIS52 |
| B | GLU56 |
| B | GLU121 |
| B | 5LD205 |
| C | HIS146 |
| C | HOH303 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | binding site for residue 5LD B 205 |
| Chain | Residue |
| B | GLU7 |
| B | HIS52 |
| B | HIS53 |
| B | GLU56 |
| B | ARG76 |
| B | ARG98 |
| B | SER171 |
| B | LYS173 |
| B | MN203 |
| B | MN204 |
| B | HOH315 |
| C | HIS29 |
| C | MET84 |
| C | HIS145 |
| C | HIS146 |
| C | GLU149 |
| C | LYS153 |
| C | HOH303 |
Functional Information from PROSITE/UniProt
| site_id | PS00955 |
| Number of Residues | 13 |
| Details | IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GeNaHHivEAaFK |
| Chain | Residue | Details |
| A | GLY141-LYS153 |
