4QC9
Crystal structure of Vaccinia virus uracil-DNA glycosylase mutant 3GD4
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 | 0006974 | biological_process | DNA damage response |
| 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 | 0006974 | biological_process | DNA damage response |
| 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 | 0006974 | biological_process | DNA damage response |
| 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 | 0006974 | biological_process | DNA damage response |
| 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | GLY159 |
| A | LYS160 |
| A | THR161 |
| A | TYR180 |
| A | HIS181 |
| A | ALA184 |
| A | HOH456 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | PHE79 |
| A | ASN120 |
| A | HOH413 |
| A | PRO69 |
| A | TYR70 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | GLN55 |
| A | ASN59 |
| A | LYS60 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | TYR11 |
| A | THR12 |
| D | GLU196 |
| D | ASN199 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 305 |
| Chain | Residue |
| A | GLU32 |
| A | SER35 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 301 |
| Chain | Residue |
| C | GLY159 |
| C | LYS160 |
| C | THR161 |
| C | TYR180 |
| C | HIS181 |
| C | ALA184 |
| C | HOH434 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 302 |
| Chain | Residue |
| C | ASP68 |
| C | PRO69 |
| C | TYR70 |
| C | PHE79 |
| C | ASN120 |
| C | HOH403 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 301 |
| Chain | Residue |
| D | GLY159 |
| D | LYS160 |
| D | THR161 |
| D | GLY179 |
| D | TYR180 |
| D | HIS181 |
| D | HOH438 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 302 |
| Chain | Residue |
| D | PRO69 |
| D | TYR70 |
| D | PRO78 |
| D | PHE79 |
| D | ASN120 |
| D | HOH405 |
| D | HOH416 |
| D | HOH439 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 301 |
| Chain | Residue |
| A | ILE103 |
| B | GLY159 |
| B | LYS160 |
| B | THR161 |
| B | TYR180 |
| B | HIS181 |
| B | HOH412 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | SER81 |
| B | PRO82 |
| B | ASN83 |
| B | PHE84 |
| B | THR85 |
| B | LYS86 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| A | LYS90 |
| B | LYS87 |
| B | ARG185 |
| B | HOH405 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 304 |
| Chain | Residue |
| B | ARG185 |
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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10072","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
