1PKJ
Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006226 | biological_process | dUMP biosynthetic process |
| A | 0006229 | biological_process | dUTP biosynthetic process |
| A | 0008829 | molecular_function | dCTP deaminase activity |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033973 | molecular_function | dCTP deaminase (dUMP-forming) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006226 | biological_process | dUMP biosynthetic process |
| B | 0006229 | biological_process | dUTP biosynthetic process |
| B | 0008829 | molecular_function | dCTP deaminase activity |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033973 | molecular_function | dCTP deaminase (dUMP-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DUT B 250 |
| Chain | Residue |
| B | ASP33 |
| B | ILE142 |
| B | THR143 |
| B | GLU145 |
| B | ARG160 |
| B | GLN163 |
| B | HOH506 |
| B | HOH511 |
| B | ARG117 |
| B | SER118 |
| B | SER119 |
| B | ARG122 |
| B | HIS128 |
| B | ILE134 |
| B | ASP135 |
| B | PHE138 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 298 |
| Chain | Residue |
| A | ASP174 |
| A | TYR177 |
| A | SER178 |
| A | HOH466 |
| B | LYS60 |
| B | LYS62 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 299 |
| Chain | Residue |
| B | ARG16 |
| B | GLU105 |
| B | LEU106 |
| B | PRO107 |
| B | HOH370 |
| B | HOH480 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P28248, ECO:0000255|HAMAP-Rule:MF_00146 |
| Chain | Residue | Details |
| A | GLU145 | |
| B | GLU145 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146 |
| Chain | Residue | Details |
| B | ARG117 | |
| B | GLN163 | |
| A | ARG117 | |
| A | GLN163 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12909016 |
| Chain | Residue | Details |
| A | HIS128 | |
| B | HIS128 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|Ref.6 |
| Chain | Residue | Details |
| A | GLY132 | |
| B | GLY132 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|Ref.6 |
| Chain | Residue | Details |
| A | LYS184 | |
| A | GLN188 | |
| B | ASP135 | |
| B | TYR177 | |
| B | LYS184 | |
| B | GLN188 | |
| A | ASP135 | |
| A | TYR177 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:12909016, ECO:0000305|Ref.6 |
| Chain | Residue | Details |
| A | THR143 | |
| B | THR143 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Important for bifunctional activity => ECO:0000255|HAMAP-Rule:MF_00146 |
| Chain | Residue | Details |
| A | GLY132 | |
| B | GLY132 |
