Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006281 | biological_process | DNA repair |
A | 0006284 | biological_process | base-excision repair |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
A | 0097510 | biological_process | base-excision repair, AP site formation via deaminated base removal |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue URA A 301 |
Chain | Residue |
A | GLN67 |
A | HOH529 |
A | ASP68 |
A | TYR70 |
A | SER80 |
A | PHE81 |
A | ASN127 |
A | HIS191 |
A | ACT305 |
A | GOL306 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue DMS A 302 |
Chain | Residue |
A | GLY39 |
A | ARG41 |
A | GLY203 |
A | SER204 |
A | ARG205 |
A | ARG209 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue DMS A 303 |
Chain | Residue |
A | ARG41 |
A | TYR42 |
A | GLU212 |
A | HOH600 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue DMS A 304 |
Chain | Residue |
A | GLN67 |
A | HIS191 |
A | SER196 |
A | CL311 |
A | HOH401 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue ACT A 305 |
Chain | Residue |
A | TYR70 |
A | ARG92 |
A | SER93 |
A | URA301 |
A | GOL306 |
A | GOL310 |
A | HOH405 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue GOL A 306 |
Chain | Residue |
A | GLN67 |
A | ASP68 |
A | PRO71 |
A | SER93 |
A | PRO137 |
A | HIS191 |
A | URA301 |
A | ACT305 |
A | HOH421 |
A | HOH549 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue GOL A 307 |
Chain | Residue |
A | GLU19 |
A | PRO20 |
A | ALA22 |
A | ASP23 |
A | HOH402 |
A | HOH635 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 308 |
Chain | Residue |
A | PRO108 |
A | ARG225 |
A | PRO227 |
A | HOH455 |
A | HOH630 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL A 309 |
Chain | Residue |
A | ASN112 |
A | ASP114 |
A | PRO117 |
A | PRO227 |
A | HOH444 |
A | HOH566 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL A 310 |
Chain | Residue |
A | ASP58 |
A | TYR70 |
A | PRO71 |
A | THR72 |
A | HIS75 |
A | PRO91 |
A | ARG92 |
A | ACT305 |
A | HOH405 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue CL A 311 |
Chain | Residue |
A | GLY169 |
A | ARG170 |
A | DMS304 |
A | HOH425 |
A | HOH539 |
Functional Information from PROSITE/UniProt
site_id | PS00130 |
Number of Residues | 10 |
Details | U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVLIvGQDPY |
Chain | Residue | Details |
A | ARG61-TYR70 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP68 | |