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 | 0016020 | cellular_component | membrane |
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 | 0016020 | cellular_component | membrane |
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 | 0016020 | cellular_component | membrane |
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 |
A | PHE103-THR110 | |
C | PHE103-THR110 |
site_id | PS00181 |
Number of Residues | 17 |
Details | GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPIinag.NGTGeHptqS |
Chain | Residue | Details |
A | LYS175-SER191 | |
C | LYS175-SER191 |