5JX0
Temperature sensitive D4 mutant L110F
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 | 7 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | GLY66 |
A | ASP68 |
A | TYR70 |
A | PRO78 |
A | PHE79 |
A | ASN120 |
A | HOH404 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CL A 302 |
Chain | Residue |
A | LYS160 |
A | HIS181 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue GOL B 301 |
Chain | Residue |
B | GLY66 |
B | ASP68 |
B | PRO69 |
B | PHE79 |
B | SER88 |
B | ASN120 |
B | HIS181 |
B | HOH410 |
B | HOH433 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL B 302 |
Chain | Residue |
B | LYS160 |
B | HIS181 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue GOL C 301 |
Chain | Residue |
C | GLY66 |
C | ILE67 |
C | ASP68 |
C | PRO69 |
C | TYR70 |
C | PHE79 |
C | ASN120 |
C | HOH404 |
C | HOH414 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL C 302 |
Chain | Residue |
C | LYS160 |
C | HIS181 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL D 301 |
Chain | Residue |
D | GLY66 |
D | ASP68 |
D | PRO69 |
D | TYR70 |
D | PHE79 |
D | ASN120 |
D | HOH409 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue CL D 302 |
Chain | Residue |
D | LYS160 |
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 |