6PNZ
The structure of the Aspartate Transcarbamoylase trimer from Staphylococcus aureus complexed with PALA at 2.27 Resolution.
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 | 15 |
| Details | binding site for residue PAL A 301 |
| Chain | Residue |
| A | SER48 |
| A | PRO252 |
| A | ALA253 |
| A | HOH410 |
| A | HOH440 |
| B | SER75 |
| B | LYS78 |
| A | THR49 |
| A | ARG50 |
| A | THR51 |
| A | ARG100 |
| A | HIS127 |
| A | ARG160 |
| A | ARG210 |
| A | GLN212 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue PAL B 301 |
| Chain | Residue |
| B | SER48 |
| B | THR49 |
| B | ARG50 |
| B | THR51 |
| B | ARG100 |
| B | HIS127 |
| B | ARG160 |
| B | ARG210 |
| B | GLN212 |
| B | ALA253 |
| B | HOH410 |
| B | HOH421 |
| B | HOH422 |
| C | SER75 |
| C | LYS78 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue PAL C 301 |
| Chain | Residue |
| A | SER75 |
| A | LYS78 |
| C | SER48 |
| C | THR49 |
| C | ARG50 |
| C | THR51 |
| C | ARG100 |
| C | HIS127 |
| C | ARG160 |
| C | ARG210 |
| C | GLN212 |
| C | PRO252 |
| C | ALA253 |
| C | HOH404 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEnSTRT |
| Chain | Residue | Details |
| A | PHE44-THR51 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001 |
| Chain | Residue | Details |
| A | ARG50 | |
| A | PRO254 | |
| B | ARG50 | |
| B | THR51 | |
| B | LYS78 | |
| B | ARG100 | |
| B | HIS127 | |
| B | GLN130 | |
| B | ARG160 | |
| B | ARG210 | |
| B | ALA253 | |
| A | THR51 | |
| B | PRO254 | |
| C | ARG50 | |
| C | THR51 | |
| C | LYS78 | |
| C | ARG100 | |
| C | HIS127 | |
| C | GLN130 | |
| C | ARG160 | |
| C | ARG210 | |
| C | ALA253 | |
| A | LYS78 | |
| C | PRO254 | |
| A | ARG100 | |
| A | HIS127 | |
| A | GLN130 | |
| A | ARG160 | |
| A | ARG210 | |
| A | ALA253 |
