Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004170 | molecular_function | dUTP diphosphatase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006226 | biological_process | dUMP biosynthetic process |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046081 | biological_process | dUTP catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070207 | biological_process | protein homotrimerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 999 |
| Chain | Residue |
| A | DUP777 |
| A | HOH1019 |
| A | HOH1045 |
| A | HOH1079 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 801 |
| Chain | Residue |
| A | HOH1044 |
| A | HOH1106 |
| A | HOH1119 |
| A | ARG34 |
| A | GLU115 |
| A | ARG116 |
| A | HOH1026 |
| A | HOH1026 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE DUP A 777 |
| Chain | Residue |
| A | MET68 |
| A | ARG71 |
| A | SER72 |
| A | GLY73 |
| A | ASN84 |
| A | GLY87 |
| A | LEU88 |
| A | ASP90 |
| A | TYR93 |
| A | MET98 |
| A | GLN119 |
| A | MG999 |
| A | HOH1000 |
| A | HOH1001 |
| A | HOH1014 |
| A | HOH1019 |
| A | HOH1020 |
| A | HOH1027 |
| A | HOH1045 |
| A | HOH1050 |
| A | HOH1051 |
| A | HOH1056 |
| A | HOH1065 |
| A | HOH1069 |
| A | HOH1073 |
| A | HOH1079 |
| A | HOH1149 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TRS A 800 |
| Chain | Residue |
| A | TRP102 |
| A | ARG104 |
| A | HOH1043 |
| A | HOH1097 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15208312","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dup |
| Chain | Residue | Details |
| A | ASP90 | |
| A | ASP92 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 844 |
| Chain | Residue | Details |
| A | SER28 | activator |
| A | PRO70 | electrostatic stabiliser |
| A | SER72 | electrostatic stabiliser |
| A | GLY79 | modifies pKa |
| A | ILE89 | proton acceptor, proton donor |
