6PK4
cryoEM structure of the substrate-bound human CTP synthase 2 filament
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003883 | molecular_function | CTP synthase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006220 | biological_process | pyrimidine nucleotide metabolic process |
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 | 0019637 | biological_process | organophosphate metabolic process |
A | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
A | 0097268 | cellular_component | cytoophidium |
B | 0003883 | molecular_function | CTP synthase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006220 | biological_process | pyrimidine nucleotide metabolic process |
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 | 0019637 | biological_process | organophosphate metabolic process |
B | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
B | 0097268 | cellular_component | cytoophidium |
C | 0003883 | molecular_function | CTP synthase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006220 | biological_process | pyrimidine nucleotide metabolic process |
C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
C | 0006241 | biological_process | CTP biosynthetic process |
C | 0006541 | biological_process | glutamine metabolic process |
C | 0016874 | molecular_function | ligase activity |
C | 0019637 | biological_process | organophosphate metabolic process |
C | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
C | 0042802 | molecular_function | identical protein binding |
C | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
C | 0097268 | cellular_component | cytoophidium |
D | 0003883 | molecular_function | CTP synthase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006220 | biological_process | pyrimidine nucleotide metabolic process |
D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
D | 0006241 | biological_process | CTP biosynthetic process |
D | 0006541 | biological_process | glutamine metabolic process |
D | 0016874 | molecular_function | ligase activity |
D | 0019637 | biological_process | organophosphate metabolic process |
D | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
D | 0042802 | molecular_function | identical protein binding |
D | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
D | 0097268 | cellular_component | cytoophidium |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue UTP A 601 |
Chain | Residue |
A | SER12 |
B | LYS195 |
B | LYS229 |
C | GLN112 |
A | LYS38 |
A | TYR42 |
A | HIS55 |
A | ASP70 |
A | GLY149 |
A | ATP602 |
B | LYS193 |
B | THR194 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue ATP A 602 |
Chain | Residue |
A | LYS16 |
A | GLY17 |
A | ILE18 |
A | LYS38 |
A | ASP70 |
A | GLU146 |
A | ARG217 |
A | VAL253 |
A | ASP312 |
A | UTP601 |
B | THR189 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue ATP B 602 |
Chain | Residue |
A | THR189 |
B | LYS16 |
B | GLY17 |
B | ILE18 |
B | LYS38 |
B | ASP70 |
B | GLU146 |
B | ARG217 |
B | VAL253 |
B | ASP312 |
B | UTP601 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue ATP C 602 |
Chain | Residue |
C | LYS16 |
C | GLY17 |
C | ILE18 |
C | LYS38 |
C | ASP70 |
C | GLU146 |
C | ARG217 |
C | VAL253 |
C | ASP312 |
C | UTP601 |
D | THR189 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue ATP D 602 |
Chain | Residue |
C | THR189 |
D | LYS16 |
D | GLY17 |
D | ILE18 |
D | LYS38 |
D | ASP70 |
D | GLU146 |
D | ARG217 |
D | VAL253 |
D | ASP312 |
D | UTP601 |
site_id | AC6 |
Number of Residues | 15 |
Details | binding site for Di-peptide UTP B 601 and HIS B 55 |
Chain | Residue |
A | LYS193 |
A | THR194 |
A | LYS195 |
A | LYS229 |
B | SER12 |
B | LYS38 |
B | TYR42 |
B | TYR53 |
B | GLU54 |
B | GLY56 |
B | ASP68 |
B | ASP70 |
B | GLY149 |
B | ATP602 |
D | GLN112 |
site_id | AC7 |
Number of Residues | 15 |
Details | binding site for Di-peptide UTP B 601 and HIS B 55 |
Chain | Residue |
A | LYS193 |
A | THR194 |
A | LYS195 |
A | LYS229 |
B | SER12 |
B | LYS38 |
B | TYR42 |
B | TYR53 |
B | GLU54 |
B | GLY56 |
B | ASP68 |
B | ASP70 |
B | GLY149 |
B | ATP602 |
D | GLN112 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for Di-peptide UTP C 601 and HIS C 55 |
Chain | Residue |
D | LYS195 |
D | LYS229 |
A | GLN112 |
C | SER12 |
C | LYS38 |
C | TYR42 |
C | TYR53 |
C | GLU54 |
C | GLY56 |
C | ASP68 |
C | ASP70 |
C | GLY149 |
C | ATP602 |
D | LYS193 |
D | THR194 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for Di-peptide UTP C 601 and HIS C 55 |
Chain | Residue |
A | GLN112 |
C | SER12 |
C | LYS38 |
C | TYR42 |
C | TYR53 |
C | GLU54 |
C | GLY56 |
C | ASP68 |
C | ASP70 |
C | GLY149 |
C | ATP602 |
D | LYS193 |
D | THR194 |
D | LYS195 |
D | LYS229 |
site_id | AD1 |
Number of Residues | 15 |
Details | binding site for Di-peptide UTP D 601 and HIS D 55 |
Chain | Residue |
B | GLN112 |
C | LYS193 |
C | THR194 |
C | LYS195 |
C | LYS229 |
D | SER12 |
D | LYS38 |
D | TYR42 |
D | TYR53 |
D | GLU54 |
D | GLY56 |
D | ASP68 |
D | ASP70 |
D | GLY149 |
D | ATP602 |
site_id | AD2 |
Number of Residues | 15 |
Details | binding site for Di-peptide UTP D 601 and HIS D 55 |
Chain | Residue |
B | GLN112 |
C | LYS193 |
C | THR194 |
C | LYS195 |
C | LYS229 |
D | SER12 |
D | LYS38 |
D | TYR42 |
D | TYR53 |
D | GLU54 |
D | GLY56 |
D | ASP68 |
D | ASP70 |
D | GLY149 |
D | ATP602 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: For GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605 |
Chain | Residue | Details |
A | CYS399 | |
D | CYS399 | |
D | HIS526 | |
D | GLU528 | |
A | HIS526 | |
A | GLU528 | |
B | CYS399 | |
B | HIS526 | |
B | GLU528 | |
C | CYS399 | |
C | HIS526 | |
C | GLU528 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER568 | |
B | SER568 | |
C | SER568 | |
D | SER568 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER571 | |
B | SER571 | |
C | SER571 | |
D | SER571 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER574 | |
B | SER574 | |
C | SER574 | |
D | SER574 |