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 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 | 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 |