4ZDJ
Crystal structure of the M. tuberculosis CTP synthase PyrG in complex with two UTP molecules
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003883 | molecular_function | CTP synthase activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| 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 | 0042802 | molecular_function | identical protein binding |
| A | 0044210 | biological_process | 'de novo' CTP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097268 | cellular_component | cytoophidium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue UTP A 601 |
| Chain | Residue |
| A | SER20 |
| A | LYS201 |
| A | GLN204 |
| A | LYS235 |
| A | MG603 |
| A | HOH715 |
| A | HOH737 |
| A | HOH756 |
| A | HOH801 |
| A | HOH812 |
| A | HOH835 |
| A | GLN120 |
| A | HOH850 |
| A | HOH884 |
| A | VAL121 |
| A | ILE122 |
| A | ASP159 |
| A | ILE160 |
| A | GLU161 |
| A | LYS199 |
| A | THR200 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue UTP A 602 |
| Chain | Residue |
| A | SER21 |
| A | LEU22 |
| A | GLY23 |
| A | LYS24 |
| A | LEU26 |
| A | THR27 |
| A | PRO194 |
| A | ARG223 |
| A | THR250 |
| A | ASP252 |
| A | ALA253 |
| A | ILE256 |
| A | ILE259 |
| A | MG604 |
| A | HOH701 |
| A | HOH702 |
| A | HOH703 |
| A | HOH722 |
| A | HOH732 |
| A | HOH745 |
| A | HOH778 |
| A | HOH781 |
| A | HOH798 |
| A | HOH819 |
| A | HOH901 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | UTP601 |
| A | HOH801 |
| A | HOH850 |
| A | HOH884 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 604 |
| Chain | Residue |
| A | UTP602 |
| A | HOH701 |
| A | HOH702 |
| A | HOH722 |
| A | HOH901 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 605 |
| Chain | Residue |
| A | PRO60 |
| A | PHE61 |
| A | ALA316 |
| A | TYR317 |
| A | GLY365 |
| A | PHE367 |
| A | HOH750 |
| A | HOH791 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A7E5","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
