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 | 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 | 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 | 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 | |