3NPM
Crystal Structure of the C47A/A241C disulfide-linked C6 Aspartate Transcarbamoylase enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
| A | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0006541 | biological_process | glutamine metabolic process |
| A | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0070207 | biological_process | protein homotrimerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 311 |
| Chain | Residue |
| A | SER52 |
| A | HOH493 |
| A | THR53 |
| A | ARG54 |
| A | THR55 |
| A | SER80 |
| A | LYS84 |
| A | ARG105 |
| A | LEU267 |
| A | PO4312 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 312 |
| Chain | Residue |
| A | THR55 |
| A | LYS84 |
| A | ARG105 |
| A | HIS134 |
| A | ARG167 |
| A | THR168 |
| A | LEU267 |
| A | PO4311 |
| A | HOH330 |
| A | HOH332 |
| A | HOH493 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT |
| Chain | Residue | Details |
| A | PHE48-THR55 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3380787","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 405 |
| Chain | Residue | Details |
| A | ARG54 | electrostatic stabiliser |
| A | THR55 | electrostatic stabiliser, increase electrophilicity |
| A | LYS84 | proton shuttle (general acid/base) |
| A | ARG105 | electrostatic stabiliser, increase electrophilicity |
| A | HIS134 | electrostatic stabiliser, increase electrophilicity |
