2AD5
Mechanisms of feedback regulation and drug resistance of CTP synthetases: structure of the E. coli CTPS/CTP complex at 2.8-Angstrom resolution.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003883 | molecular_function | CTP synthase activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006241 | biological_process | CTP biosynthetic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0097268 | cellular_component | cytoophidium |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003883 | molecular_function | CTP synthase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006241 | biological_process | CTP biosynthetic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0097268 | cellular_component | cytoophidium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 701 |
| Chain | Residue |
| A | GLY19 |
| A | LYS40 |
| A | ASP72 |
| A | GLU140 |
| A | ADP601 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1701 |
| Chain | Residue |
| B | GLY19 |
| B | ASP72 |
| B | GLU140 |
| B | ADP1601 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP A 601 |
| Chain | Residue |
| A | SER15 |
| A | LEU16 |
| A | GLY17 |
| A | LYS18 |
| A | GLY19 |
| A | ILE20 |
| A | ASP72 |
| A | GLU140 |
| A | ARG211 |
| A | LYS239 |
| A | VAL241 |
| A | MG701 |
| A | HOH722 |
| B | ALA182 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP B 1601 |
| Chain | Residue |
| A | ALA182 |
| B | SER15 |
| B | LEU16 |
| B | GLY17 |
| B | LYS18 |
| B | GLY19 |
| B | ILE20 |
| B | ASP72 |
| B | GLU140 |
| B | LEU238 |
| B | LYS239 |
| B | ASP240 |
| B | VAL241 |
| B | ILE247 |
| B | MG1701 |
| B | HOH1761 |
| B | HOH1801 |
| B | HOH1821 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CTP A 602 |
| Chain | Residue |
| A | SER14 |
| A | GLN114 |
| A | VAL115 |
| A | ILE116 |
| A | ASP147 |
| A | ILE148 |
| A | GLU149 |
| A | HOH711 |
| A | HOH745 |
| A | HOH783 |
| A | HOH788 |
| B | LYS187 |
| B | THR188 |
| B | LYS189 |
| B | GLN192 |
| B | LYS223 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CTP B 1602 |
| Chain | Residue |
| A | VAL186 |
| A | LYS187 |
| A | THR188 |
| A | LYS189 |
| A | GLN192 |
| A | LYS223 |
| B | SER14 |
| B | GLN114 |
| B | VAL115 |
| B | ILE116 |
| B | ASP147 |
| B | ILE148 |
| B | GLU149 |
| B | HOH1752 |
| B | HOH1754 |
| B | HOH1759 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile; for glutamine hydrolysis => ECO:0000305|PubMed:11336655, ECO:0000305|PubMed:15157079 |
| Chain | Residue | Details |
| A | LEU380 | |
| B | LEU380 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:15157079 |
| Chain | Residue | Details |
| A | PRO516 | |
| A | PHE518 | |
| B | PRO516 | |
| B | PHE518 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16216072 |
| Chain | Residue | Details |
| A | SER15 | |
| A | THR188 | |
| A | ILE224 | |
| B | SER15 | |
| B | THR188 | |
| B | ILE224 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16216072, ECO:0007744|PDB:2AD5 |
| Chain | Residue | Details |
| A | LEU16 | |
| A | ILE148 | |
| A | ASP240 | |
| B | LEU16 | |
| B | ILE148 | |
| B | ASP240 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16216072, ECO:0007744|PDB:2AD5 |
| Chain | Residue | Details |
| A | LEU73 | |
| A | ILE141 | |
| B | LEU73 | |
| B | ILE141 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01227 |
| Chain | Residue | Details |
| A | PHE353 | |
| A | GLY381 | |
| A | PHE404 | |
| A | TYR471 | |
| B | PHE353 | |
| B | GLY381 | |
| B | PHE404 | |
| B | TYR471 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | CYS379 | |
| A | HIS515 | |
| A | GLU517 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | CYS379 | |
| B | HIS515 | |
| B | GLU517 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | CYS379 | |
| A | HIS515 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | CYS379 | |
| B | HIS515 |
