1AT1
CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H
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 |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
| C | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| 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 | 0006541 | biological_process | glutamine metabolic process |
| C | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| C | 0070207 | biological_process | protein homotrimerization |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MLI A 312 |
| Chain | Residue |
| A | LYS84 |
| A | HIS134 |
| A | ARG167 |
| A | THR168 |
| A | ARG229 |
| A | GLN231 |
| A | PCT311 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MLI C 312 |
| Chain | Residue |
| C | LYS84 |
| C | ARG105 |
| C | HIS134 |
| C | ARG167 |
| C | THR168 |
| C | ARG229 |
| C | GLN231 |
| C | PRO268 |
| C | PCT311 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 154 |
| Chain | Residue |
| B | CYS109 |
| B | CYS114 |
| B | CYS138 |
| B | CYS141 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 154 |
| Chain | Residue |
| D | CYS109 |
| D | CYS114 |
| D | CYS138 |
| D | CYS141 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PCT A 311 |
| Chain | Residue |
| A | SER52 |
| A | THR53 |
| A | ARG54 |
| A | THR55 |
| A | SER80 |
| A | LYS84 |
| A | ARG105 |
| A | HIS134 |
| A | GLN137 |
| A | PRO266 |
| A | LEU267 |
| A | MLI312 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PCT C 311 |
| Chain | Residue |
| C | ALA51 |
| C | SER52 |
| C | THR53 |
| C | ARG54 |
| C | THR55 |
| C | SER80 |
| C | LYS84 |
| C | ARG105 |
| C | HIS134 |
| C | GLN137 |
| C | LEU267 |
| C | MLI312 |
| site_id | PMA |
| Number of Residues | 10 |
| Details | BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A |
| Chain | Residue |
| A | ARG54 |
| A | LEU267 |
| A | THR55 |
| A | ARG105 |
| A | HIS134 |
| A | GLN137 |
| A | ARG167 |
| A | ARG229 |
| A | GLN231 |
| A | PRO266 |
| site_id | PMC |
| Number of Residues | 10 |
| Details | BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C |
| Chain | Residue |
| C | ARG54 |
| C | THR55 |
| C | ARG105 |
| C | HIS134 |
| C | GLN137 |
| C | ARG167 |
| C | ARG229 |
| C | GLN231 |
| C | PRO266 |
| C | LEU267 |
| site_id | ZNB |
| Number of Residues | 4 |
| Details | ZN BINDING SITES OF CHAINS B |
| Chain | Residue |
| B | CYS109 |
| B | CYS114 |
| B | CYS138 |
| B | CYS141 |
| site_id | ZND |
| Number of Residues | 4 |
| Details | ZN BINDING SITES OF CHAINS D |
| Chain | Residue |
| D | CYS109 |
| D | CYS114 |
| D | CYS138 |
| D | CYS141 |
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 | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | PRO110 | |
| C | HIS106 | |
| C | PRO135 | |
| C | THR138 | |
| C | PRO268 | |
| C | ARG269 | |
| B | ILE115 | |
| B | LYS139 | |
| B | GLU142 | |
| D | PRO110 | |
| D | ILE115 | |
| D | LYS139 | |
| D | GLU142 | |
| C | ARG56 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 |
| Chain | Residue | Details |
| A | GLY85 | |
| A | THR168 | |
| A | VAL230 | |
| C | GLY85 | |
| C | THR168 | |
| C | VAL230 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 10651286 |
| Chain | Residue | Details |
| A | ARG105 | |
| A | HIS134 | |
| A | THR55 | |
| A | LYS84 | |
| A | ARG54 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 405 |
| Chain | Residue | Details |
| A | THR55 | electrostatic stabiliser |
| A | ARG56 | electrostatic stabiliser, increase electrophilicity |
| A | GLY85 | proton shuttle (general acid/base) |
| A | HIS106 | electrostatic stabiliser, increase electrophilicity |
| A | PRO135 | electrostatic stabiliser, increase electrophilicity |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 405 |
| Chain | Residue | Details |
| C | THR55 | electrostatic stabiliser |
| C | ARG56 | electrostatic stabiliser, increase electrophilicity |
| C | GLY85 | proton shuttle (general acid/base) |
| C | HIS106 | electrostatic stabiliser, increase electrophilicity |
| C | PRO135 | electrostatic stabiliser, increase electrophilicity |
