1EUG
CRYSTAL STRUCTURE OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE AND ITS COMPLEXES WITH URACIL AND GLYCEROL: STRUCTURE AND GLYCOSYLASE MECHANISM REVISITED
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 | 0006974 | biological_process | DNA damage response |
| 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 |
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 | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10805771, 10946228 |
| Chain | Residue | Details |
| A | PHE77 | |
| A | HIS187 | |
| A | TYR66 |
| 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 | HIS187 | covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
