3R7D
Crystal Structure of Unliganded Aspartate Transcarbamoylase from Bacillus subtilis
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 | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 A 305 |
| Chain | Residue |
| A | ASN67 |
| B | ASN67 |
| B | HOH313 |
| C | ASN67 |
| A | HOH319 |
| A | HOH323 |
| A | HOH328 |
| A | HOH334 |
| A | HOH367 |
| A | HOH385 |
| A | HOH388 |
| A | HOH411 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 306 |
| Chain | Residue |
| A | SER11 |
| A | THR12 |
| A | ARG171 |
| A | HOH312 |
| A | HOH343 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 307 |
| Chain | Residue |
| A | THR73 |
| A | SER74 |
| A | LYS77 |
| C | SER47 |
| C | THR48 |
| C | ARG49 |
| C | PRO251 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 305 |
| Chain | Residue |
| B | SER11 |
| B | THR12 |
| B | ARG171 |
| B | HOH372 |
| B | HOH484 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 305 |
| Chain | Residue |
| C | LYS272 |
| C | LYS275 |
| C | HOH357 |
| C | HOH381 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 306 |
| Chain | Residue |
| C | SER11 |
| C | THR12 |
| C | ARG171 |
| C | HOH359 |
| C | HOH573 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEpSTRT |
| Chain | Residue | Details |
| A | PHE43-THR50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
