Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000703 | molecular_function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003684 | molecular_function | damaged DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| A | 0006281 | biological_process | DNA repair |
| A | 0006284 | biological_process | base-excision repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019104 | molecular_function | DNA N-glycosylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | CYS237 |
| A | CYS240 |
| A | CYS257 |
| A | CYS260 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 302 |
| Chain | Residue |
| A | HIS184 |
| A | HIS262 |
| A | HIS262 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 303 |
| Chain | Residue |
| A | HIS220 |
| A | ASP195 |
| A | HIS199 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 304 |
| Chain | Residue |
| A | GLU173 |
| A | TRP176 |
| A | LYS228 |
Functional Information from PROSITE/UniProt
| site_id | PS01242 |
| Number of Residues | 25 |
| Details | ZF_FPG_1 Zinc finger FPG-type signature. Cer..CGsiIekttlss....RPfyWCpgCQ |
| Chain | Residue | Details |
| A | CYS237-GLN261 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | Zinc finger: {"description":"FPG-type"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor; for beta-elimination activity","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor; for delta-elimination activity","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11847126","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1k82 |
| Chain | Residue | Details |
| A | LYS52 | |
| A | ARG252 | |
