1OX6
TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | histidine biosynthetic process |
| A | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| B | 0000105 | biological_process | histidine biosynthetic process |
| B | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016833 | molecular_function | oxo-acid-lyase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI B 901 |
| Chain | Residue |
| B | GLY-3 |
| B | SER-2 |
| B | HIS-1 |
| B | MET1 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 902 |
| Chain | Residue |
| A | HIS-1 |
| A | GLY-3 |
| A | SER-2 |
| A | MET1 |
| B | TYR425 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 801 |
| Chain | Residue |
| A | GLY364 |
| A | THR365 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 802 |
| Chain | Residue |
| A | GLY475 |
| A | SER500 |
| A | GLY501 |
| A | HOH961 |
| A | HOH1034 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 803 |
| Chain | Residue |
| B | LYS158 |
| B | LYS170 |
| B | LYS343 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 804 |
| Chain | Residue |
| B | GLY331 |
| B | GLY364 |
| B | THR365 |
| B | HOH1107 |
| B | HOH1126 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 806 |
| Chain | Residue |
| A | SER130 |
| A | ASN132 |
| A | HOH1027 |
| B | LYS493 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE POP B 999 |
| Chain | Residue |
| B | ASP474 |
| B | GLY475 |
| B | ASN477 |
| B | SER500 |
| B | GLY501 |
| B | GLY524 |
| B | MET525 |
| B | ARG528 |
| B | HOH1013 |
| B | HOH1050 |
| B | HOH1095 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TISKAYGAQA |
| Chain | Residue | Details |
| A | THR389-ALA398 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: For GATase activity => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS83 | |
| A | HIS193 | |
| A | GLU195 | |
| B | CYS83 | |
| B | HIS193 | |
| B | GLU195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| A | ASP245 | |
| A | ASP404 | |
| B | ASP245 | |
| B | ASP404 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: covalent |
| Chain | Residue | Details |
| A | CYS83 | |
| B | CYS83 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY332 | |
| A | ASN469 | |
| B | GLY332 | |
| B | ASN469 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | GLU195 | |
| A | CYS83 | |
| A | HIS193 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | GLU195 | |
| B | CYS83 | |
| B | HIS193 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | CYS83 | |
| A | HIS193 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | CYS83 | |
| B | HIS193 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | ASP245 | |
| A | ASP404 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | ASP245 | |
| B | ASP404 |
