6HDE
Structure of Escherichia coli dUTPase Q93H mutant
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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004170 | molecular_function | dUTP diphosphatase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006226 | biological_process | dUMP biosynthetic process |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046081 | biological_process | dUTP catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070207 | biological_process | protein homotrimerization |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004170 | molecular_function | dUTP diphosphatase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006226 | biological_process | dUMP biosynthetic process |
| C | 0009117 | biological_process | nucleotide metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046081 | biological_process | dUTP catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070207 | biological_process | protein homotrimerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue DUP A 201 |
| Chain | Residue |
| A | ARG71 |
| A | HOH311 |
| A | HOH325 |
| A | HOH333 |
| A | HOH339 |
| A | HOH343 |
| B | ASN84 |
| B | GLY87 |
| B | LEU88 |
| B | ILE89 |
| B | ASP90 |
| A | SER72 |
| B | TYR93 |
| B | MET98 |
| A | GLY73 |
| A | GLN119 |
| A | MG203 |
| A | HOH303 |
| A | HOH306 |
| A | HOH308 |
| A | HOH309 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue DUP A 202 |
| Chain | Residue |
| A | ARG141 |
| A | GLY145 |
| A | PHE146 |
| A | GLY147 |
| A | HIS148 |
| A | SER149 |
| A | HOH301 |
| A | HOH310 |
| A | HOH332 |
| A | HOH334 |
| A | HOH341 |
| B | ARG71 |
| B | SER72 |
| B | GLY73 |
| B | GLN119 |
| B | MG202 |
| B | HOH302 |
| B | HOH314 |
| C | ASN84 |
| C | GLY87 |
| C | LEU88 |
| C | ASP90 |
| C | TYR93 |
| C | MET98 |
| C | HOH303 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 203 |
| Chain | Residue |
| A | DUP201 |
| A | HOH308 |
| A | HOH311 |
| A | HOH339 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue DUP B 201 |
| Chain | Residue |
| A | ASN84 |
| A | GLY87 |
| A | LEU88 |
| A | ILE89 |
| A | ASP90 |
| A | TYR93 |
| A | MET98 |
| A | HOH302 |
| B | ARG141 |
| B | GLY145 |
| B | PHE146 |
| B | GLY147 |
| B | HIS148 |
| B | SER149 |
| B | HOH303 |
| B | HOH311 |
| B | HOH315 |
| B | HOH341 |
| C | ARG71 |
| C | SER72 |
| C | GLY73 |
| C | GLN119 |
| C | MG201 |
| C | HOH305 |
| C | HOH318 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| A | DUP202 |
| A | HOH334 |
| B | HOH302 |
| B | HOH314 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 201 |
| Chain | Residue |
| B | DUP201 |
| B | HOH341 |
| C | HOH305 |
| C | HOH318 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Motif: {"description":"Motif 5, important for activity","evidences":[{"source":"PubMed","id":"9261872","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15208312","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| 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 |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 844 |
| Chain | Residue | Details |
| B | SER28 | activator |
| B | PRO70 | electrostatic stabiliser |
| B | SER72 | electrostatic stabiliser |
| B | GLY79 | modifies pKa |
| B | ILE89 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 844 |
| Chain | Residue | Details |
| C | SER28 | activator |
| C | PRO70 | electrostatic stabiliser |
| C | SER72 | electrostatic stabiliser |
| C | GLY79 | modifies pKa |
| C | ILE89 | proton acceptor, proton donor |
