1UPU
STRUCTURE OF THE URACIL PHOSPHORIBOSYLTRANSFERASE, MUTANT C128V, BOUND TO PRODUCT URIDINE-1-MONOPHOSPHATE (UMP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009507 | cellular_component | chloroplast |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0044206 | biological_process | UMP salvage |
| A | 0050262 | molecular_function | ribosylnicotinamide kinase activity |
| B | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009507 | cellular_component | chloroplast |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0044206 | biological_process | UMP salvage |
| B | 0050262 | molecular_function | ribosylnicotinamide kinase activity |
| C | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009507 | cellular_component | chloroplast |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0044206 | biological_process | UMP salvage |
| C | 0050262 | molecular_function | ribosylnicotinamide kinase activity |
| D | 0004845 | molecular_function | uracil phosphoribosyltransferase activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009507 | cellular_component | chloroplast |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0044206 | biological_process | UMP salvage |
| D | 0050262 | molecular_function | ribosylnicotinamide kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 899 |
| Chain | Residue |
| B | LYS59 |
| D | LYS104 |
| D | ARG129 |
| D | ARG158 |
| D | HOH1012 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 899 |
| Chain | Residue |
| C | HOH1087 |
| A | LYS59 |
| C | LYS104 |
| C | ARG129 |
| C | ARG158 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 899 |
| Chain | Residue |
| B | LYS104 |
| B | ARG129 |
| B | ARG158 |
| B | HOH1000 |
| B | HOH1033 |
| D | LYS59 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 899 |
| Chain | Residue |
| A | LYS104 |
| A | ARG129 |
| A | ARG158 |
| A | HOH1002 |
| A | HOH1036 |
| A | HOH1041 |
| C | LYS59 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE U5P D 999 |
| Chain | Residue |
| D | ARG137 |
| D | ASP164 |
| D | MET166 |
| D | ALA168 |
| D | THR169 |
| D | ALA170 |
| D | GLY171 |
| D | SER172 |
| D | TYR228 |
| D | ILE229 |
| D | GLY234 |
| D | ASP235 |
| D | PHE236 |
| D | HOH1008 |
| D | HOH1035 |
| D | HOH1056 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE U5P C 999 |
| Chain | Residue |
| C | ARG137 |
| C | ASP164 |
| C | MET166 |
| C | ALA168 |
| C | THR169 |
| C | ALA170 |
| C | GLY171 |
| C | SER172 |
| C | TYR228 |
| C | ILE229 |
| C | GLY234 |
| C | ASP235 |
| C | PHE236 |
| C | HOH1005 |
| C | HOH1006 |
| C | HOH1036 |
| C | HOH1106 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE U5P B 999 |
| Chain | Residue |
| B | ALA113 |
| B | ARG137 |
| B | ASP164 |
| B | MET166 |
| B | ALA168 |
| B | THR169 |
| B | ALA170 |
| B | GLY171 |
| B | SER172 |
| B | TYR228 |
| B | ILE229 |
| B | GLY234 |
| B | ASP235 |
| B | PHE236 |
| B | HOH1002 |
| B | HOH1007 |
| B | HOH1082 |
| C | HOH1119 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE U5P A 999 |
| Chain | Residue |
| A | ASP164 |
| A | MET166 |
| A | ALA168 |
| A | THR169 |
| A | ALA170 |
| A | GLY171 |
| A | SER172 |
| A | TYR228 |
| A | ILE229 |
| A | GLY234 |
| A | ASP235 |
| A | PHE236 |
| A | HOH1019 |
| A | HOH1026 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9628859, ECO:0007744|PDB:1BD3, ECO:0007744|PDB:1UPU |
| Chain | Residue | Details |
| D | LYS59 | |
| C | LYS59 | |
| B | LYS59 | |
| A | LYS59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11773618, ECO:0007744|PDB:1JLR |
| Chain | Residue | Details |
| D | ARG68 | |
| D | TYR102 | |
| C | ARG68 | |
| C | TYR102 | |
| B | ARG68 | |
| B | TYR102 | |
| A | ARG68 | |
| A | TYR102 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11773618, ECO:0007744|PDB:1JLS |
| Chain | Residue | Details |
| D | ARG112 | |
| C | ARG112 | |
| B | ARG112 | |
| A | ARG112 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11773618, ECO:0000269|PubMed:9628859, ECO:0007744|PDB:1BD3, ECO:0007744|PDB:1BD4, ECO:0007744|PDB:1JLR, ECO:0007744|PDB:1JLS, ECO:0007744|PDB:1UPU |
| Chain | Residue | Details |
| D | ARG129 | |
| A | ARG129 | |
| A | ARG137 | |
| A | ARG158 | |
| D | ARG137 | |
| D | ARG158 | |
| C | ARG129 | |
| C | ARG137 | |
| C | ARG158 | |
| B | ARG129 | |
| B | ARG137 | |
| B | ARG158 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11773618, ECO:0000269|PubMed:9628859, ECO:0007744|PDB:1JLS, ECO:0007744|PDB:1UPU |
| Chain | Residue | Details |
| D | ASP164 | |
| C | ASP164 | |
| B | ASP164 | |
| A | ASP164 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9628859, ECO:0007744|PDB:1UPU |
| Chain | Residue | Details |
| D | ILE229 | |
| D | GLY234 | |
| C | ILE229 | |
| C | GLY234 | |
| B | ILE229 | |
| B | GLY234 | |
| A | ILE229 | |
| A | GLY234 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11773618, ECO:0007744|PDB:1JLR, ECO:0007744|PDB:1JLS |
| Chain | Residue | Details |
| D | ASP235 | |
| C | ASP235 | |
| B | ASP235 | |
| A | ASP235 |
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 |
| D | ARG137 | electrostatic stabiliser |
| D | THR141 | electrostatic stabiliser |
| D | ASP235 | electrostatic stabiliser |
| D | ASP238 | modifies pKa |
| site_id | MCSA2 |
| 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 | MCSA3 |
| 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 | MCSA4 |
| 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 |
