1KXJ
The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009382 | cellular_component | imidazoleglycerol-phosphate synthase complex |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009382 | cellular_component | imidazoleglycerol-phosphate synthase complex |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 204 |
| Chain | Residue |
| A | GLY52 |
| A | GLN88 |
| A | GLU96 |
| A | HIS141 |
| A | THR142 |
| A | TYR143 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 204 |
| Chain | Residue |
| B | THR142 |
| B | TYR143 |
| B | GLN88 |
| B | GLU96 |
| B | HIS141 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 205 |
| Chain | Residue |
| A | GLY11 |
| A | ARG60 |
| B | LYS101 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 206 |
| Chain | Residue |
| A | GLU150 |
| A | PO4207 |
| B | ARG59 |
| B | GLU63 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 205 |
| Chain | Residue |
| A | GLU92 |
| A | GLU107 |
| B | GLY11 |
| B | ARG60 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 207 |
| Chain | Residue |
| A | GLU150 |
| A | HIS151 |
| A | LYS169 |
| A | PO4206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 199 |
| Details | Domain: {"description":"Glutamine amidotransferase type-1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | GLU180 | |
| A | CYS84 | |
| A | HIS178 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | GLU180 | |
| B | CYS84 | |
| B | HIS178 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | CYS84 | |
| A | HIS178 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | CYS84 | |
| B | HIS178 |
