6FBA
Crystal Structure of truncated aspartate transcarbamoylase from Plasmodium falciparum with bound inhibitor 2,3-naphthalenediol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| C | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
| C | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | GLY122 |
| A | LYS124 |
| B | LYS124 |
| B | SO4401 |
| C | GLY122 |
| C | LYS124 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue D48 A 402 |
| Chain | Residue |
| A | LEU149 |
| A | TYR152 |
| B | ARG109 |
| B | PRO335 |
| A | GLU140 |
| A | ALA145 |
| A | ILE148 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 403 |
| Chain | Residue |
| A | THR77 |
| A | ILE84 |
| A | TYR93 |
| A | TYR368 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue MLI A 404 |
| Chain | Residue |
| A | ARG109 |
| A | THR110 |
| A | SER113 |
| A | GLN190 |
| A | PRO333 |
| A | ARG363 |
| A | HOH505 |
| A | HOH509 |
| C | TYR152 |
| C | D48401 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MLI A 405 |
| Chain | Residue |
| A | SER107 |
| A | THR108 |
| A | ARG109 |
| A | THR110 |
| A | ARG295 |
| C | LYS138 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | PHE103 |
| A | GLU105 |
| A | SER107 |
| A | THR108 |
| A | ARG111 |
| A | THR129 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 407 |
| Chain | Residue |
| A | HOH517 |
| A | HOH529 |
| B | HOH535 |
| B | HOH541 |
| C | HOH509 |
| C | HOH556 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| A | LEU119 |
| A | LYS124 |
| A | SO4401 |
| B | LEU119 |
| B | LYS124 |
| B | HOH504 |
| B | HOH505 |
| B | HOH514 |
| C | LEU119 |
| C | LYS124 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue D48 B 402 |
| Chain | Residue |
| B | GLU140 |
| B | ALA145 |
| B | ILE148 |
| B | LEU149 |
| B | TYR152 |
| B | HOH527 |
| C | ARG109 |
| C | LEU334 |
| C | PRO335 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 403 |
| Chain | Residue |
| B | ILE84 |
| B | TYR368 |
| B | HOH538 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue PEG B 404 |
| Chain | Residue |
| B | GLY139 |
| B | THR141 |
| B | ASP144 |
| C | ARG336 |
| C | VAL337 |
| C | VAL342 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue D48 C 401 |
| Chain | Residue |
| A | ARG109 |
| A | LEU334 |
| A | MLI404 |
| C | GLU140 |
| C | ILE148 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue DMS C 402 |
| Chain | Residue |
| C | TYR368 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue PEG C 403 |
| Chain | Residue |
| A | VAL342 |
| A | ASP345 |
| C | THR141 |
| C | GLU143 |
| C | ASP144 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue MLI C 404 |
| Chain | Residue |
| B | LYS138 |
| C | PRO106 |
| C | SER107 |
| C | THR108 |
| C | ARG109 |
| C | THR110 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 405 |
| Chain | Residue |
| C | ARG325 |
| C | ASP326 |
| C | ASP327 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FlEpSTRT |
| Chain | Residue | Details |
| C | PHE103-THR110 | |
| A | PHE103-THR110 |
| site_id | PS00181 |
| Number of Residues | 17 |
| Details | GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPIinag.NGTGeHptqS |
| Chain | Residue | Details |
| C | LYS175-SER191 | |
| A | LYS175-SER191 |
