Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0097510 | biological_process | base-excision repair, AP site formation via deaminated base removal |
| B | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0097510 | biological_process | base-excision repair, AP site formation via deaminated base removal |
| C | 0005515 | molecular_function | protein binding |
| D | 0005515 | molecular_function | protein binding |
Functional Information from PDB Data
| site_id | GB1 |
| Number of Residues | 1 |
| Details | GENERAL BASE TO ACTIVATE NUCLEOPHILIC WATER |
| site_id | GB2 |
| Number of Residues | 1 |
| Details | GENERAL BASE TO ACTIVATE NUCLEOPHILIC WATER |
| site_id | UR1 |
| Number of Residues | 4 |
| Details | URACIL BINDING RESIDUES BY HOMOLOGY |
| Chain | Residue |
| A | GLN63 |
| A | TYR66 |
| A | PHE77 |
| A | ASN123 |
| site_id | UR2 |
| Number of Residues | 4 |
| Details | URACIL BINDING RESIDUES BY HOMOLOGY |
| Chain | Residue |
| B | GLN63 |
| B | TYR66 |
| B | PHE77 |
| B | ASN123 |
Functional Information from PROSITE/UniProt
| site_id | PS00130 |
| Number of Residues | 10 |
| Details | U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY |
| Chain | Residue | Details |
| A | LYS57-TYR66 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | ASP64 | |
| B | ASP64 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eug |
| Chain | Residue | Details |
| A | ASP187 | |
| A | ASP64 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eug |
| Chain | Residue | Details |
| B | ASP187 | |
| B | ASP64 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 71 |
| Chain | Residue | Details |
| A | ASP64 | activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor |
| A | TYR66 | activator, steric role |
| A | PHE77 | activator, steric role |
| A | ASP187 | covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 71 |
| Chain | Residue | Details |
| B | ASP64 | activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor |
| B | TYR66 | activator, steric role |
| B | PHE77 | activator, steric role |
| B | ASP187 | covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
