6L6S
The structure of the UdgX mutant H109E crosslinked to single-stranded DNA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006281 | biological_process | DNA repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0097506 | molecular_function | deaminated base DNA N-glycosylase activity |
| B | 0006281 | biological_process | DNA repair |
| B | 0006974 | biological_process | DNA damage response |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0097506 | molecular_function | deaminated base DNA N-glycosylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 A 301 |
| Chain | Residue |
| A | CYS24 |
| A | GLY26 |
| A | CYS27 |
| A | HIS95 |
| A | CYS120 |
| A | TRP123 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 301 |
| Chain | Residue |
| B | TYR30 |
| B | HIS95 |
| B | CYS120 |
| B | TRP123 |
| B | CYS24 |
| B | GLY26 |
| B | CYS27 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | binding site for Poly-Saccharide residues DG C 7 through GLU A 109 |
| Chain | Residue |
| A | ALA4 |
| A | GLN5 |
| A | ASP6 |
| A | HIS10 |
| A | THR11 |
| A | GLU23 |
| A | ARG25 |
| A | GLU52 |
| A | GLN53 |
| A | PRO68 |
| A | ALA69 |
| A | PHE96 |
| A | LYS97 |
| A | ILE108 |
| A | LYS110 |
| A | TRP123 |
| A | ALA126 |
| A | HIS178 |
| A | SER180 |
| A | SER181 |
| A | LEU183 |
| A | ARG184 |
| A | HOH408 |
| A | HOH413 |
| A | HOH415 |
| A | HOH418 |
| A | HOH464 |
| A | HOH467 |
| C | DT6 |
| C | DG10 |
| C | HOH104 |
| C | HOH106 |
| C | HOH108 |
| C | HOH119 |
| C | HOH122 |
| C | HOH123 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | binding site for Di-Saccharide ORP C 8 and DA C 9 |
| Chain | Residue |
| A | ALA4 |
| A | GLN5 |
| A | ASP6 |
| A | PHE7 |
| A | HIS10 |
| A | THR11 |
| A | GLU52 |
| A | GLN53 |
| A | PRO68 |
| A | ALA69 |
| A | PHE96 |
| A | LYS97 |
| A | ILE108 |
| A | LYS110 |
| A | ALA126 |
| A | HIS178 |
| A | SER180 |
| A | SER181 |
| A | ARG184 |
| A | HOH408 |
| A | HOH413 |
| A | HOH415 |
| A | HOH418 |
| A | HOH467 |
| C | DG7 |
| C | DG10 |
| C | HOH104 |
| C | HOH122 |
| C | HOH123 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | binding site for Poly-Saccharide residues DG D 7 through GLU B 109 |
| Chain | Residue |
| D | HOH110 |
| D | HOH113 |
| D | HOH114 |
| B | GLU52 |
| B | GLN53 |
| B | PRO54 |
| B | GLY55 |
| B | GLY67 |
| B | PRO68 |
| B | ALA69 |
| B | PHE96 |
| B | LYS97 |
| B | ILE108 |
| B | LYS110 |
| B | HIS178 |
| B | SER180 |
| B | SER181 |
| B | LEU183 |
| B | ARG184 |
| B | HOH417 |
| D | DT6 |
| D | DG10 |
| D | HOH102 |
| D | HOH104 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for Di-Saccharide ORP D 8 and DA D 9 |
| Chain | Residue |
| B | GLY67 |
| B | PRO68 |
| B | ALA69 |
| B | GLU109 |
| B | HIS178 |
| B | SER180 |
| B | SER181 |
| B | ARG184 |
| B | HOH417 |
| D | DG7 |
| D | DG10 |
| D | HOH102 |
| D | HOH109 |
| D | HOH110 |
| D | HOH113 |
| D | HOH114 |
