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 | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 997 |
| Chain | Residue |
| A | DUD777 |
| A | HOH1021 |
| A | HOH1025 |
| A | HOH1044 |
| A | HOH1133 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE DUD A 777 |
| Chain | Residue |
| A | ASN84 |
| A | GLY87 |
| A | LEU88 |
| A | ASP90 |
| A | TYR93 |
| A | MET98 |
| A | GLN119 |
| A | MN997 |
| A | HOH998 |
| A | HOH999 |
| A | HOH1002 |
| A | HOH1005 |
| A | HOH1021 |
| A | HOH1025 |
| A | HOH1104 |
| A | HOH1115 |
| A | HOH1133 |
| A | HOH1150 |
| A | MET68 |
| A | ARG71 |
| A | SER72 |
| A | GLY73 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | LYS3 |
| A | LYS3 |
| A | LYS4 |
| A | LYS4 |
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 |
