3QTY
Crystal structure of Phosphoribosylaminoimidazole Synthetase from Francisella tularensis complexed with pyrophosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004637 | molecular_function | phosphoribosylamine-glycine ligase activity |
| A | 0004641 | molecular_function | phosphoribosylformylglycinamidine cyclo-ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046084 | biological_process | adenine biosynthetic process |
| B | 0004637 | molecular_function | phosphoribosylamine-glycine ligase activity |
| B | 0004641 | molecular_function | phosphoribosylformylglycinamidine cyclo-ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046084 | biological_process | adenine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | GLY68 |
| A | HOH507 |
| B | HOH442 |
| A | THR69 |
| A | ASN192 |
| A | GLY193 |
| A | TYR194 |
| A | SER195 |
| A | HOH357 |
| A | HOH441 |
| A | HOH502 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS A 401 |
| Chain | Residue |
| A | ASN234 |
| A | ILE235 |
| A | HIS327 |
| A | THR328 |
| A | ASN329 |
| A | THR330 |
| A | HOH370 |
| A | HOH459 |
| B | HOH545 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE POP A 403 |
| Chain | Residue |
| A | LYS113 |
| A | LYS275 |
| A | ALA279 |
| A | THR280 |
| A | LYS285 |
| A | HOH486 |
| A | HOH524 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE POP A 404 |
| Chain | Residue |
| A | PHE42 |
| A | ASP107 |
| A | MSE119 |
| A | VAL123 |
| A | MSE126 |
| A | LEU137 |
| A | GLY140 |
| A | HOH562 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 405 |
| Chain | Residue |
| A | PRO146 |
| A | LYS331 |
| A | HOH387 |
| A | HOH449 |
| B | GLN150 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 402 |
| Chain | Residue |
| A | MSE145 |
| A | PRO146 |
| A | GLY147 |
| A | HOH387 |
| B | THR69 |
| B | SER195 |
| B | ARG198 |
| B | HOH578 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS B 400 |
| Chain | Residue |
| A | ASN340 |
| B | ASN234 |
| B | HIS327 |
| B | ASN329 |
| B | HOH407 |
| B | HOH462 |
| B | HOH464 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE POP B 401 |
| Chain | Residue |
| B | ASP107 |
| B | MSE119 |
| B | VAL123 |
| B | LEU137 |
| B | GLY139 |
| B | GLY140 |
| B | THR142 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 348 |
| Chain | Residue |
| B | GLY68 |
| B | THR69 |
| B | ASN192 |
| B | GLY193 |
| B | TYR194 |
| B | SER195 |
| B | HOH385 |
| B | HOH457 |
| B | HOH574 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 403 |
| Chain | Residue |
| B | ASN192 |
| B | THR253 |
| B | GLY254 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 404 |
| Chain | Residue |
| B | ALA279 |
| B | THR280 |
| B | LYS285 |
| B | HOH368 |
