2D3Y
Crystal structure of uracil-DNA glycosylase from Thermus Thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| 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 | 0033958 | molecular_function | DNA-deoxyinosine glycosylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0097506 | molecular_function | deaminated base DNA N-glycosylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 222 |
| Chain | Residue |
| A | ALA59 |
| A | SER65 |
| A | PRO71 |
| A | PHE72 |
| A | HOH230 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 223 |
| Chain | Residue |
| A | HOH228 |
| A | GLY151 |
| A | ARG152 |
| A | HIS190 |
| A | ASN195 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 220 |
| Chain | Residue |
| A | CYS13 |
| A | LEU15 |
| A | CYS16 |
| A | LEU19 |
| A | PRO42 |
| A | CYS115 |
| A | CYS130 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DU A 221 |
| Chain | Residue |
| A | TRP22 |
| A | GLU25 |
| A | PHE46 |
| A | GLY47 |
| A | ASP48 |
| A | LEU102 |
| A | ARG103 |
| A | LEU104 |
| A | HOH247 |
| A | HOH304 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"Structure of family 5 uracil-DNA glycosylase bound to DNA reveals insights into the mechanism for substrate recognition and catalysis.","authors":["Kosaka H.","Nakagawa N.","Masui R.","Kuramitsu S."]}},{"source":"PDB","id":"2D3Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DDG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DEM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1mug |
| Chain | Residue | Details |
| A | ALA59 |
