1BD3
STRUCTURE OF THE APO URACIL PHOSPHORIBOSYLTRANSFERASE, 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 PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 D 799 |
| Chain | Residue |
| D | LYS104 |
| D | HOH937 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 799 |
| Chain | Residue |
| C | ARG137 |
| C | ALA168 |
| C | THR169 |
| C | ALA170 |
| C | GLY171 |
| C | SER172 |
| C | HOH904 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 899 |
| Chain | Residue |
| A | LYS59 |
| C | LYS104 |
| C | ARG129 |
| C | ARG158 |
| C | HOH979 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 799 |
| Chain | Residue |
| B | ARG137 |
| B | CYS167 |
| B | ALA168 |
| B | THR169 |
| B | ALA170 |
| B | GLY171 |
| B | SER172 |
| B | HOH909 |
| B | HOH991 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 899 |
| Chain | Residue |
| B | LYS104 |
| B | ARG129 |
| B | ARG158 |
| B | HOH900 |
| B | HOH935 |
| D | LYS59 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 799 |
| Chain | Residue |
| A | ARG137 |
| A | ALA168 |
| A | THR169 |
| A | ALA170 |
| A | GLY171 |
| A | SER172 |
| A | HOH926 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 899 |
| Chain | Residue |
| A | LYS104 |
| A | ARG129 |
| A | ARG158 |
| A | HOH941 |
| C | LYS59 |
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 | a catalytic site defined by CSA, PubMed 9628859 |
| Chain | Residue | Details |
| A | THR141 | |
| A | ARG137 | |
| A | ASP235 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9628859 |
| Chain | Residue | Details |
| D | THR141 | |
| D | ARG137 | |
| D | ASP235 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9628859 |
| Chain | Residue | Details |
| C | THR141 | |
| C | ARG137 | |
| C | ASP235 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9628859 |
| Chain | Residue | Details |
| B | THR141 | |
| B | ARG137 | |
| B | 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 |
