1S1M
Crystal Structure of E. Coli CTP Synthetase
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 | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 602 |
Chain | Residue |
A | SER15 |
A | GLY17 |
A | LYS18 |
A | GLY19 |
A | SO4603 |
A | MG702 |
A | HOH908 |
A | HOH970 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 603 |
Chain | Residue |
A | LYS40 |
A | GLU140 |
A | GLY142 |
A | GLY143 |
A | SO4602 |
A | MG702 |
A | MG703 |
A | HOH872 |
A | LYS18 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 1602 |
Chain | Residue |
B | SER15 |
B | LEU16 |
B | GLY17 |
B | LYS18 |
B | GLY19 |
B | MG701 |
B | HOH1688 |
B | HOH1690 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1603 |
Chain | Residue |
B | LYS18 |
B | LYS40 |
B | GLY142 |
B | GLY143 |
B | MG701 |
B | MG704 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 701 |
Chain | Residue |
B | GLY19 |
B | ASP72 |
B | GLU140 |
B | SO41602 |
B | SO41603 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 702 |
Chain | Residue |
A | GLY19 |
A | LYS40 |
A | ASP72 |
A | GLU140 |
A | SO4602 |
A | SO4603 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 703 |
Chain | Residue |
A | LYS40 |
A | ASP42 |
A | PRO43 |
A | SO4603 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 704 |
Chain | Residue |
B | LYS40 |
B | ASP42 |
B | SO41603 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 801 |
Chain | Residue |
A | SER237 |
A | LYS239 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 802 |
Chain | Residue |
B | SER237 |
B | LYS239 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 804 |
Chain | Residue |
B | GLU163 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 805 |
Chain | Residue |
A | LYS233 |
A | LYS262 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 806 |
Chain | Residue |
A | PRO178 |
B | PRO178 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 807 |
Chain | Residue |
A | HOH979 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 808 |
Chain | Residue |
B | LYS189 |
B | HOH1754 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 810 |
Chain | Residue |
B | VAL241 |
B | ASP242 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 811 |
Chain | Residue |
B | HOH1871 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 812 |
Chain | Residue |
A | VAL241 |
A | ASP242 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IOD A 813 |
Chain | Residue |
A | GLU64 |
A | VAL464 |
A | ARG466 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IOD A 814 |
Chain | Residue |
A | HIS193 |
B | HIS193 |
B | HOH1735 |
site_id | CC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 815 |
Chain | Residue |
B | ARG466 |
B | HOH1774 |
site_id | CC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 816 |
Chain | Residue |
B | HIS193 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD A 601 |
Chain | Residue |
A | ARG211 |
A | LYS239 |
A | ASP240 |
A | VAL241 |
A | ILE244 |
B | ALA182 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD B 1601 |
Chain | Residue |
B | ARG211 |
B | LEU238 |
B | LYS239 |
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 |