7OLI
Crystal structure of Pab-AGOG in complex with 8-oxoguanosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000702 | molecular_function | oxidized base lesion DNA N-glycosylase activity |
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 | 0016787 | molecular_function | hydrolase activity |
A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
A | 0016829 | molecular_function | lyase activity |
A | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
B | 0000702 | molecular_function | oxidized base lesion DNA N-glycosylase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
B | 0006281 | biological_process | DNA repair |
B | 0006284 | biological_process | base-excision repair |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
B | 0016829 | molecular_function | lyase activity |
B | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue 8HG A 301 |
Chain | Residue |
A | GLN24 |
A | ASP208 |
A | TRP212 |
A | HOH449 |
A | HOH465 |
A | HOH515 |
A | SER51 |
A | TYR52 |
A | TRP62 |
A | LYS142 |
A | PHE146 |
A | LYS149 |
A | PRO172 |
A | ASP174 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | ARG15 |
A | GLU19 |
A | ARG156 |
A | SER160 |
A | THR161 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue 8HG B 301 |
Chain | Residue |
B | GLN24 |
B | SER51 |
B | TYR52 |
B | TRP62 |
B | LYS142 |
B | PHE146 |
B | PRO172 |
B | ASP174 |
B | ASP208 |
B | TRP212 |
B | HOH435 |
B | HOH474 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | GLU19 |
B | ARG29 |
B | GLU233 |
B | LYS236 |
B | HOH404 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | ARG15 |
B | GLU19 |
B | ARG156 |
B | SER160 |
B | THR161 |
B | HOH445 |
B | HOH521 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | LYS57 |
B | GLY58 |
B | ARG176 |
B | HOH474 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | MET1 |
B | ARG4 |
B | ASN20 |
B | SER222 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with DNA => ECO:0000255|HAMAP-Rule:MF_01168 |
Chain | Residue | Details |
A | LYS142 | |
B | LYS142 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01168 |
Chain | Residue | Details |
A | ASP174 | |
B | ASP174 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01168 |
Chain | Residue | Details |
A | GLN24 | |
B | TRP62 | |
B | PHE146 | |
B | PRO172 | |
B | ASP208 | |
B | TRP212 | |
A | SER51 | |
A | TRP62 | |
A | PHE146 | |
A | PRO172 | |
A | ASP208 | |
A | TRP212 | |
B | GLN24 | |
B | SER51 |