5U3C
CryoEM structure of the CTP synthase filament at 4.6 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003883 | molecular_function | CTP synthase activity |
| C | 0004359 | molecular_function | glutaminase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| C | 0006241 | biological_process | CTP biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0097268 | cellular_component | cytoophidium |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003883 | molecular_function | CTP synthase activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| D | 0006241 | biological_process | CTP biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0097268 | cellular_component | cytoophidium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue CTP A 601 |
| Chain | Residue |
| A | ASP147 |
| A | ILE148 |
| A | GLU149 |
| B | GLN114 |
| B | VAL115 |
| B | ILE116 |
| C | THR188 |
| C | LYS189 |
| C | LYS196 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue ADP A 602 |
| Chain | Residue |
| A | LEU16 |
| A | GLY17 |
| A | LYS18 |
| A | ILE20 |
| A | ASP72 |
| A | ARG211 |
| A | LYS239 |
| A | ASP240 |
| A | VAL241 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue CTP B 601 |
| Chain | Residue |
| A | GLN114 |
| B | SER14 |
| B | ASP147 |
| B | ILE148 |
| B | GLU149 |
| D | THR188 |
| D | LYS189 |
| D | LYS196 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue ADP B 602 |
| Chain | Residue |
| B | LEU16 |
| B | GLY17 |
| B | LYS18 |
| B | GLY19 |
| B | ILE20 |
| B | ARG211 |
| B | LYS239 |
| B | ASP240 |
| B | VAL241 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue CTP C 601 |
| Chain | Residue |
| A | THR188 |
| A | LYS189 |
| A | LYS196 |
| C | SER14 |
| C | ASP147 |
| C | ILE148 |
| C | GLU149 |
| D | GLN114 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue ADP C 602 |
| Chain | Residue |
| C | LEU16 |
| C | GLY17 |
| C | LYS18 |
| C | GLY19 |
| C | ILE20 |
| C | ASP72 |
| C | ARG211 |
| C | LYS239 |
| C | ASP240 |
| C | VAL241 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue CTP D 601 |
| Chain | Residue |
| B | THR188 |
| B | LYS189 |
| B | LYS196 |
| C | ILE116 |
| D | SER14 |
| D | ASP147 |
| D | ILE148 |
| D | GLU149 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue ADP D 602 |
| Chain | Residue |
| D | LEU16 |
| D | GLY17 |
| D | LYS18 |
| D | GLY19 |
| D | ILE20 |
| D | ARG211 |
| D | LYS239 |
| D | ASP240 |
| D | VAL241 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1060 |
| Details | Region: {"description":"Amidoligase domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"source":"PubMed","id":"11336655","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15157079","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"15157079","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16216072","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16216072","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2AD5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16216072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AD5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1056 |
| Details | Region: {"description":"Amidoligase domain","evidences":[{"source":"PubMed","id":"15157079","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






