5TKV
X-RAY CRYSTAL STRUCTURE OF THE "CLOSED" CONFORMATION OF CTP-INHIBITED E. COLI CYTIDINE TRIPHOSPHATE (CTP) SYNTHETASE
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 | 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 | 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 | 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 | 13 |
| Details | binding site for residue GLN A 601 |
| Chain | Residue |
| A | GLY351 |
| A | ARG470 |
| A | TYR471 |
| A | HIS515 |
| A | HOH799 |
| A | GLY352 |
| A | PHE353 |
| A | CYS379 |
| A | LEU380 |
| A | GLN383 |
| A | GLU403 |
| A | ARG468 |
| A | HIS469 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | LEU16 |
| A | GLY17 |
| A | LYS18 |
| A | GLY19 |
| A | SO4603 |
| A | HOH701 |
| A | HOH779 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | LYS18 |
| A | LYS40 |
| A | GLU140 |
| A | GLY142 |
| A | GLY143 |
| A | SO4602 |
| A | HOH702 |
| A | HOH770 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MPD A 604 |
| Chain | Residue |
| A | ARG211 |
| A | VAL241 |
| A | ILE247 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | ARG391 |
| A | HIS392 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | LYS297 |
| A | PHE353 |
| A | ARG356 |
| A | HOH704 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 607 |
| Chain | Residue |
| B | CTP603 |
| B | HOH788 |
| B | HOH821 |
| B | HOH841 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue CTP B 601 |
| Chain | Residue |
| A | SER14 |
| A | GLN114 |
| A | ILE116 |
| A | ASP147 |
| A | ILE148 |
| A | GLU149 |
| A | HOH730 |
| B | LYS187 |
| B | THR188 |
| B | LYS189 |
| B | GLN192 |
| B | LYS223 |
| B | MG602 |
| B | HOH759 |
| B | HOH771 |
| B | HOH785 |
| B | HOH796 |
| B | HOH799 |
| B | HOH812 |
| B | HOH837 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 602 |
| Chain | Residue |
| B | CTP601 |
| B | HOH796 |
| B | HOH812 |
| B | HOH837 |
| site_id | AD1 |
| Number of Residues | 20 |
| Details | binding site for residue CTP B 603 |
| Chain | Residue |
| A | LYS187 |
| A | THR188 |
| A | LYS189 |
| A | GLN192 |
| A | LYS223 |
| A | MG607 |
| B | SER14 |
| B | GLN114 |
| B | VAL115 |
| B | ILE116 |
| B | ASP147 |
| B | ILE148 |
| B | GLU149 |
| B | HOH728 |
| B | HOH740 |
| B | HOH788 |
| B | HOH795 |
| B | HOH809 |
| B | HOH821 |
| B | HOH841 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue GLN B 604 |
| Chain | Residue |
| B | GLY351 |
| B | GLY352 |
| B | PHE353 |
| B | CYS379 |
| B | LEU380 |
| B | GLN383 |
| B | GLU403 |
| B | HIS469 |
| B | ARG470 |
| B | TYR471 |
| B | HIS515 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 605 |
| Chain | Residue |
| B | LYS18 |
| B | GLY19 |
| B | SO4606 |
| B | HOH704 |
| B | HOH738 |
| B | SER15 |
| B | LEU16 |
| B | GLY17 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 606 |
| Chain | Residue |
| B | LYS18 |
| B | LYS40 |
| B | GLU140 |
| B | GLY142 |
| B | GLY143 |
| B | SO4605 |
| B | HOH703 |
| B | HOH705 |
| B | HOH847 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue MPD B 607 |
| Chain | Residue |
| B | ARG211 |
| B | LEU238 |
| B | LYS239 |
| B | ASP240 |
| B | VAL241 |
| B | ILE247 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 608 |
| Chain | Residue |
| B | ARG391 |
| B | HIS392 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 609 |
| Chain | Residue |
| B | LYS297 |
| B | ARG356 |
| B | HOH701 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue MRD B 611 |
| Chain | Residue |
| B | GLU283 |
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 | CYS379 | |
| B | CYS379 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:15157079 |
| Chain | Residue | Details |
| A | HIS515 | |
| A | GLU517 | |
| B | HIS515 | |
| B | GLU517 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16216072 |
| Chain | Residue | Details |
| A | SER14 | |
| A | LYS187 | |
| A | LYS223 | |
| B | SER14 | |
| B | LYS187 | |
| B | LYS223 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16216072, ECO:0007744|PDB:2AD5 |
| Chain | Residue | Details |
| A | SER15 | |
| A | ASP147 | |
| A | LYS239 | |
| B | SER15 | |
| B | ASP147 | |
| B | LYS239 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16216072, ECO:0007744|PDB:2AD5 |
| Chain | Residue | Details |
| A | ASP72 | |
| A | GLU140 | |
| B | ASP72 | |
| B | GLU140 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01227 |
| Chain | Residue | Details |
| A | GLY352 | |
| A | LEU380 | |
| A | GLU403 | |
| A | ARG470 | |
| B | GLY352 | |
| B | LEU380 | |
| B | GLU403 | |
| B | ARG470 |
