1UPF
STRUCTURE OF THE URACIL PHOSPHORIBOSYLTRANSFERASE, MUTANT C128V BOUND TO THE DRUG 5-FLUOROURACIL
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 PDB Data
| site_id | AC1 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE SO4 D 799 | 
| Chain | Residue | 
| D | ARG137 | 
| D | CYS167 | 
| D | ALA168 | 
| D | THR169 | 
| D | ALA170 | 
| D | GLY171 | 
| D | SER172 | 
| site_id | AC2 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE SO4 D 599 | 
| Chain | Residue | 
| D | ARG112 | 
| D | ALA113 | 
| D | GLY237 | 
| D | HOH1005 | 
| D | HOH1019 | 
| B | LYS150 | 
| D | VAL111 | 
| site_id | AC3 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE SO4 D 899 | 
| Chain | Residue | 
| B | LYS59 | 
| D | ARG129 | 
| D | ARG158 | 
| site_id | AC4 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE SO4 C 799 | 
| Chain | Residue | 
| C | ARG137 | 
| C | ALA168 | 
| C | THR169 | 
| C | ALA170 | 
| C | GLY171 | 
| C | SER172 | 
| C | HOH1013 | 
| C | HOH1032 | 
| C | HOH1069 | 
| site_id | AC5 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE SO4 C 599 | 
| Chain | Residue | 
| C | ARG112 | 
| C | ALA113 | 
| C | GLY237 | 
| site_id | AC6 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE SO4 C 899 | 
| Chain | Residue | 
| A | LYS59 | 
| C | ARG129 | 
| C | ARG158 | 
| site_id | AC7 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE SO4 B 599 | 
| Chain | Residue | 
| B | ARG112 | 
| B | ALA113 | 
| B | GLY237 | 
| B | HOH1011 | 
| B | HOH1034 | 
| site_id | AC8 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE SO4 B 799 | 
| Chain | Residue | 
| B | ARG137 | 
| B | CYS167 | 
| B | ALA168 | 
| B | THR169 | 
| B | ALA170 | 
| B | GLY171 | 
| B | SER172 | 
| B | HOH1006 | 
| site_id | AC9 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE SO4 B 899 | 
| Chain | Residue | 
| B | ARG129 | 
| B | ARG158 | 
| B | HOH1000 | 
| B | HOH1005 | 
| D | LYS59 | 
| site_id | BC1 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE SO4 A 799 | 
| Chain | Residue | 
| A | ARG137 | 
| A | ALA168 | 
| A | THR169 | 
| A | ALA170 | 
| A | GLY171 | 
| A | SER172 | 
| site_id | BC2 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE SO4 A 899 | 
| Chain | Residue | 
| A | ARG129 | 
| A | ARG158 | 
| C | LYS59 | 
| site_id | BC3 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE SO4 A 599 | 
| Chain | Residue | 
| A | ARG112 | 
| A | ALA113 | 
| A | GLY237 | 
| site_id | BC4 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE URF D 999 | 
| Chain | Residue | 
| D | MET166 | 
| D | ALA168 | 
| D | TYR227 | 
| D | TYR228 | 
| D | ILE229 | 
| D | GLY234 | 
| D | PHE236 | 
| site_id | BC5 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE URF C 999 | 
| Chain | Residue | 
| C | MET166 | 
| C | ALA168 | 
| C | TYR227 | 
| C | TYR228 | 
| C | ILE229 | 
| C | GLY234 | 
| C | ASP235 | 
| C | PHE236 | 
| C | HOH1003 | 
| site_id | BC6 | 
| Number of Residues | 10 | 
| Details | BINDING SITE FOR RESIDUE URF B 999 | 
| Chain | Residue | 
| B | MET166 | 
| B | ALA168 | 
| B | TYR227 | 
| B | TYR228 | 
| B | ILE229 | 
| B | ILE233 | 
| B | GLY234 | 
| B | ASP235 | 
| B | PHE236 | 
| B | HOH1002 | 
| site_id | BC7 | 
| Number of Residues | 10 | 
| Details | BINDING SITE FOR RESIDUE URF A 999 | 
| Chain | Residue | 
| A | MET166 | 
| A | ALA168 | 
| A | TYR227 | 
| A | TYR228 | 
| A | ILE229 | 
| A | GLY234 | 
| A | ASP235 | 
| A | PHE236 | 
| A | HOH1013 | 
| A | HOH1045 | 
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 | 
| D | THR141 | |
| D | ARG137 | |
| D | ASP235 | 
| site_id | CSA2 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1bd3 | 
| Chain | Residue | Details | 
| C | THR141 | |
| C | ARG137 | |
| C | ASP235 | 
| site_id | CSA3 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1bd3 | 
| Chain | Residue | Details | 
| B | THR141 | |
| B | ARG137 | |
| B | ASP235 | 
| site_id | CSA4 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1bd3 | 
| Chain | Residue | Details | 
| A | THR141 | |
| A | ARG137 | |
| A | 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 | 4 | 
| Details | M-CSA 420 | 
| Chain | Residue | Details | 
| B | ARG137 | electrostatic stabiliser | 
| B | THR141 | electrostatic stabiliser | 
| B | ASP235 | electrostatic stabiliser | 
| B | ASP238 | modifies pKa | 
| site_id | MCSA3 | 
| Number of Residues | 4 | 
| Details | M-CSA 420 | 
| Chain | Residue | Details | 
| C | ARG137 | electrostatic stabiliser | 
| C | THR141 | 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 | 






