4YIG
vaccinia virus D4/A20(1-50) in complex with dsDNA containing an abasic site and free uracyl
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 | 0005515 | molecular_function | protein binding |
A | 0006281 | biological_process | DNA repair |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
A | 0039693 | biological_process | viral DNA genome replication |
E | 0003677 | molecular_function | DNA binding |
E | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
E | 0005515 | molecular_function | protein binding |
E | 0006281 | biological_process | DNA repair |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
E | 0039693 | biological_process | viral DNA genome replication |
I | 0003677 | molecular_function | DNA binding |
I | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
I | 0005515 | molecular_function | protein binding |
I | 0006281 | biological_process | DNA repair |
I | 0016787 | molecular_function | hydrolase activity |
I | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
I | 0039693 | biological_process | viral DNA genome replication |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue URA A 301 |
Chain | Residue |
A | GLY66 |
C | ORP5 |
A | ILE67 |
A | ASP68 |
A | TYR70 |
A | PRO78 |
A | PHE79 |
A | ASN120 |
A | HIS181 |
A | HOH402 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue URA E 301 |
Chain | Residue |
E | GLY66 |
E | ILE67 |
E | ASP68 |
E | TYR70 |
E | PRO78 |
E | PHE79 |
E | SER88 |
E | ASN120 |
E | HIS181 |
G | ORP5 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue URA I 301 |
Chain | Residue |
I | GLY66 |
I | ILE67 |
I | ASP68 |
I | TYR70 |
I | PRO78 |
I | PHE79 |
I | ASN120 |
I | HIS181 |
K | ORP5 |
site_id | AC4 |
Number of Residues | 20 |
Details | binding site for Poly-Saccharide residues DT C 4 through DA C 6 |
Chain | Residue |
A | ASP68 |
A | PRO69 |
A | TYR70 |
A | PRO71 |
A | LYS72 |
A | LYS86 |
A | LYS87 |
A | SER88 |
A | THR130 |
A | HIS181 |
A | ARG185 |
A | URA301 |
A | HOH407 |
C | DG3 |
C | DT7 |
C | HOH103 |
C | HOH102 |
D | DA25 |
D | DT26 |
D | DA28 |
site_id | AC5 |
Number of Residues | 36 |
Details | binding site for Poly-Saccharide residues DT G 4 through DA G 6 |
Chain | Residue |
A | ASP68 |
A | PRO69 |
A | TYR70 |
A | PRO71 |
A | LYS72 |
A | LYS86 |
A | LYS87 |
A | SER88 |
A | THR130 |
A | HIS181 |
A | ARG185 |
A | URA301 |
A | HOH407 |
C | DG3 |
C | DT7 |
C | HOH103 |
C | HOH102 |
D | DA25 |
D | DT26 |
D | DA28 |
E | ASP68 |
E | PRO69 |
E | TYR70 |
E | PRO71 |
E | LYS86 |
E | LYS87 |
E | SER88 |
E | THR130 |
E | HIS181 |
E | ARG185 |
E | URA301 |
G | DG3 |
G | DT7 |
H | DA25 |
H | DT26 |
H | DA28 |
site_id | AC6 |
Number of Residues | 34 |
Details | binding site for Poly-Saccharide residues DT K 4 through DA K 6 |
Chain | Residue |
H | DT26 |
H | DA28 |
I | ASP68 |
I | PRO69 |
I | TYR70 |
I | PRO71 |
I | LYS72 |
I | LYS87 |
I | SER88 |
I | THR130 |
I | HIS181 |
I | ALA183 |
I | ARG185 |
I | URA301 |
I | HOH404 |
K | DG3 |
K | DT7 |
L | DA25 |
L | DT26 |
L | DA28 |
E | ASP68 |
E | PRO69 |
E | TYR70 |
E | PRO71 |
E | LYS86 |
E | LYS87 |
E | SER88 |
E | THR130 |
E | HIS181 |
E | ARG185 |
E | URA301 |
G | DG3 |
G | DT7 |
H | DA25 |
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 | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10072 |
Chain | Residue | Details |
A | ASP68 | |
E | ASP68 | |
I | ASP68 |