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 | 3 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER72 | |
B | SER72 | |
C | SER72 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15208312 |
Chain | Residue | Details |
A | LEU85 | |
A | ILE99 | |
B | LEU85 | |
B | ILE99 | |
C | LEU85 | |
C | ILE99 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ILE89 | |
B | ILE89 | |
C | ILE89 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 844 |
Chain | Residue | Details |
A | ALA29 | activator |
A | ARG71 | electrostatic stabiliser |
A | GLY73 | electrostatic stabiliser |
A | ILE80 | modifies pKa |
A | ASP90 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 844 |
Chain | Residue | Details |
B | ALA29 | activator |
B | ARG71 | electrostatic stabiliser |
B | GLY73 | electrostatic stabiliser |
B | ILE80 | modifies pKa |
B | ASP90 | proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 844 |
Chain | Residue | Details |
C | ALA29 | activator |
C | ARG71 | electrostatic stabiliser |
C | GLY73 | electrostatic stabiliser |
C | ILE80 | modifies pKa |
C | ASP90 | proton acceptor, proton donor |