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 501 |
Chain | Residue |
A | CYS237 |
A | CYS240 |
A | CYS257 |
A | CYS260 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 551 |
Chain | Residue |
A | ARG8 |
A | ASN12 |
A | HOH657 |
A | HOH1022 |
A | HOH1025 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 552 |
Chain | Residue |
A | ARG112 |
A | LYS140 |
A | ALA191 |
A | ASP195 |
A | HOH665 |
A | HOH757 |
A | HOH856 |
A | HOH957 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 553 |
Chain | Residue |
A | ASN190 |
A | ALA191 |
A | HOH630 |
A | HOH828 |
A | HOH884 |
A | HOH941 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 554 |
Chain | Residue |
A | PRO1 |
A | HOH681 |
A | HOH961 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 555 |
Chain | Residue |
A | HOH648 |
A | HOH652 |
A | HOH734 |
A | HOH994 |
A | HOH1071 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 511 |
Chain | Residue |
A | ARG147 |
A | ARG151 |
A | HOH685 |
A | HOH773 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 512 |
Chain | Residue |
A | ASP195 |
A | HIS199 |
A | HOH684 |
A | HOH691 |
A | HOH722 |
A | HOH752 |
A | HOH932 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 513 |
Chain | Residue |
A | SER37 |
A | GLN38 |
A | GLY179 |
A | LEU180 |
A | HIS184 |
A | GLN193 |
A | HIS262 |
A | HOH671 |
A | HOH689 |
A | HOH737 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 514 |
Chain | Residue |
A | THR117 |
A | ARG142 |
A | HOH655 |
A | HOH711 |
A | HOH998 |
A | HOH1054 |
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 | 1 |
Details | ACT_SITE: Schiff-base intermediate with DNA |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor; for beta-elimination activity => ECO:0000305 |
Chain | Residue | Details |
A | ALA53 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor; for delta-elimination activity => ECO:0000305 |
Chain | Residue | Details |
A | PRO253 | |
Chain | Residue | Details |
A | LEU70 | |
A | VAL125 | |
A | TYR169 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1k82 |
Chain | Residue | Details |
A | GLU2 | |
A | LYS52 | |
A | PRO1 | |
A | ARG252 | |