4QCA
Crystal structure of Vaccinia virus uracil-DNA glycosylase mutant R167AD4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| A | 0006281 | biological_process | DNA repair |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| B | 0006281 | biological_process | DNA repair |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| C | 0003677 | molecular_function | DNA binding |
| C | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| C | 0006281 | biological_process | DNA repair |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| D | 0003677 | molecular_function | DNA binding |
| D | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| D | 0006281 | biological_process | DNA repair |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | GLY66 |
| A | HOH521 |
| A | ILE67 |
| A | ASP68 |
| A | TYR70 |
| A | PRO78 |
| A | PHE79 |
| A | ASN120 |
| A | HOH412 |
| A | HOH492 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | LYS160 |
| A | HIS181 |
| A | HOH526 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 303 |
| Chain | Residue |
| A | SER172 |
| A | VAL174 |
| A | HOH448 |
| A | HOH530 |
| A | HOH541 |
| B | HOH474 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 301 |
| Chain | Residue |
| B | LYS160 |
| B | TYR180 |
| B | HIS181 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 301 |
| Chain | Residue |
| C | GLY66 |
| C | ASP68 |
| C | TYR70 |
| C | PRO78 |
| C | PHE79 |
| C | SER88 |
| C | ASN120 |
| C | HOH402 |
| C | HOH545 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 302 |
| Chain | Residue |
| C | LYS160 |
| C | TYR180 |
| C | HIS181 |
| C | HOH541 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 301 |
| Chain | Residue |
| D | GLY66 |
| D | ASP68 |
| D | TYR70 |
| D | PRO78 |
| D | PHE79 |
| D | SER88 |
| D | ASN120 |
| D | HIS181 |
| D | HOH402 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL D 302 |
| Chain | Residue |
| C | ALA167 |
| C | ALA168 |
| C | LYS169 |
| C | LEU170 |
| C | GLU171 |
| D | ALA167 |
| D | ALA168 |
| D | LYS169 |
| D | LEU170 |
| D | GLU171 |
| D | HOH481 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 303 |
| Chain | Residue |
| D | LYS160 |
| D | TYR180 |
| D | HIS181 |
Functional Information from PROSITE/UniProt
| site_id | PS00130 |
| Number of Residues | 10 |
| Details | U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVCVcGIDPY |
| Chain | Residue | Details |
| A | ARG61-TYR70 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10072 |
| Chain | Residue | Details |
| A | ASP68 | |
| B | ASP68 | |
| C | ASP68 | |
| D | ASP68 |
