1JLS
STRUCTURE OF THE URACIL PHOSPHORIBOSYLTRANSFERASE URACIL/CPR 2 MUTANT C128V
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0008655 | biological_process | pyrimidine-containing compound salvage |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0044206 | biological_process | UMP salvage |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0008655 | biological_process | pyrimidine-containing compound salvage |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0044206 | biological_process | UMP salvage |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0008655 | biological_process | pyrimidine-containing compound salvage |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0044206 | biological_process | UMP salvage |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0008655 | biological_process | pyrimidine-containing compound salvage |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0044206 | biological_process | UMP salvage |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9628859","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BD3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UPU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11773618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JLR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11773618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JLS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11773618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9628859","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BD3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BD4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UPU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11773618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9628859","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BD3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BD4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JLS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11773618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9628859","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UPU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9628859","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UPU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11773618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JLS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd3 |
| Chain | Residue | Details |
| B | THR141 | |
| B | ARG137 | |
| B | ASP235 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd3 |
| Chain | Residue | Details |
| A | ARG137 | |
| A | ASP235 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd3 |
| Chain | Residue | Details |
| D | ARG137 | |
| D | ASP235 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd3 |
| Chain | Residue | Details |
| C | THR141 | |
| C | ARG137 | |
| C | ASP235 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 420 |
| Chain | Residue | Details |
| A | ARG137 | electrostatic stabiliser |
| A | THR141 | electrostatic stabiliser |
| A | ASP235 | electrostatic stabiliser |
| A | ASP238 | modifies pKa |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 420 |
| Chain | Residue | Details |
| B | ARG137 | electrostatic stabiliser |
| B | ASP235 | electrostatic stabiliser |
| B | ASP238 | modifies pKa |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 420 |
| Chain | Residue | Details |
| C | ARG137 | electrostatic stabiliser |
| C | ASP235 | electrostatic stabiliser |
| C | ASP238 | modifies pKa |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 420 |
| Chain | Residue | Details |
| D | ARG137 | electrostatic stabiliser |
| D | THR141 | electrostatic stabiliser |
| D | ASP235 | electrostatic stabiliser |
| D | ASP238 | modifies pKa |






