6IOD
The structure of UdgX in complex with 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 | 8 |
| Details | binding site for residue SF4 A 301 |
| Chain | Residue |
| A | CYS24 |
| A | GLY26 |
| A | CYS27 |
| A | LYS94 |
| A | HIS95 |
| A | CYS120 |
| A | TRP123 |
| A | HOH533 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 B 301 |
| Chain | Residue |
| B | GLY26 |
| B | CYS27 |
| B | HIS95 |
| B | CYS120 |
| B | CYS24 |
| site_id | AC3 |
| Number of Residues | 40 |
| Details | binding site for Poly-Saccharide residues DG C 7 through HIS A 109 |
| Chain | Residue |
| A | ALA4 |
| A | GLN5 |
| A | ASP6 |
| A | HIS10 |
| A | THR11 |
| A | ALA20 |
| A | ARG25 |
| A | GLU52 |
| A | GLN53 |
| A | PRO54 |
| A | GLY55 |
| A | PRO68 |
| A | ALA69 |
| A | ILE108 |
| A | LYS110 |
| A | TRP123 |
| A | HIS178 |
| A | SER180 |
| A | SER181 |
| A | LEU183 |
| A | ARG184 |
| A | HOH411 |
| A | HOH428 |
| A | HOH430 |
| A | HOH444 |
| A | HOH460 |
| A | HOH461 |
| A | HOH529 |
| A | HOH531 |
| C | DT6 |
| C | DG10 |
| C | DA13 |
| C | DT14 |
| C | HOH103 |
| C | HOH107 |
| C | HOH108 |
| C | HOH110 |
| C | HOH118 |
| C | HOH123 |
| C | HOH135 |
| site_id | AC4 |
| Number of Residues | 35 |
| 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 | ALA20 |
| A | GLU52 |
| A | GLN53 |
| A | PRO54 |
| A | GLY55 |
| A | PRO68 |
| A | ALA69 |
| A | ILE108 |
| A | LYS110 |
| A | HIS178 |
| A | SER180 |
| A | SER181 |
| A | ARG184 |
| A | HOH411 |
| A | HOH428 |
| A | HOH430 |
| A | HOH444 |
| A | HOH460 |
| A | HOH531 |
| C | DG7 |
| C | DG10 |
| C | DA13 |
| C | DT14 |
| C | HOH107 |
| C | HOH108 |
| C | HOH110 |
| C | HOH118 |
| C | HOH123 |
| C | HOH135 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | binding site for Poly-Saccharide residues DG D 7 through HIS B 109 |
| Chain | Residue |
| B | GLY55 |
| B | GLY67 |
| B | PRO68 |
| B | ALA69 |
| B | PHE96 |
| B | ILE108 |
| B | LYS110 |
| B | TRP123 |
| B | HIS178 |
| B | SER180 |
| B | LEU183 |
| B | ARG184 |
| B | HOH407 |
| B | HOH415 |
| B | HOH428 |
| B | HOH434 |
| B | HOH438 |
| B | HOH458 |
| D | DT6 |
| D | DG10 |
| D | HOH103 |
| D | HOH106 |
| B | ALA4 |
| B | GLN5 |
| B | ASP6 |
| B | HIS10 |
| B | THR11 |
| B | ALA20 |
| B | ARG25 |
| B | GLY26 |
| B | GLU52 |
| B | GLN53 |
| B | PRO54 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for Di-Saccharide ORP D 8 and DA D 9 |
| Chain | Residue |
| B | GLN53 |
| B | PRO54 |
| B | GLY55 |
| B | GLY67 |
| B | PRO68 |
| B | ALA69 |
| B | HIS109 |
| B | HIS178 |
| B | SER180 |
| B | ARG184 |
| B | HOH407 |
| B | HOH434 |
| D | DG7 |
| D | DG10 |
| D | HOH103 |
| D | HOH106 |
