Human Thymine DNA Glycosylase Bound to Substrate Analog 2'-fluoro-2'-deoxyuridine. Determined by X-ray diffraction at 2.97 Å resolution. Released 25 Apr 2012.
Explore 3UFJ in 3D Show helices and sheets RCSB PDB PDBe
3UFJ contains 19 α-helices and 12 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 124-126 | 3 | |
| β-strand | 134-138 | 5 | 1 |
| α-helix | 143-148 | 6 | |
| β-strand | 157 | 1 | 2 |
| α-helix | 159-166 | 8 | |
| α-helix | 175-180 | 6 | |
| α-helix | 181-185 | 5 | |
| β-strand | 187-191 | 5 | 1 |
| α-helix | 205-222 | 18 | |
| β-strand | 226-230 | 5 | 1 |
| α-helix | 232-238 | 7 | |
| α-helix | 239-243 | 5 | |
| β-strand | 253-255 | 3 | 1 |
| α-helix | 258-259 | 2 | |
| β-strand | 265-269 | 5 | 1 |
| β-strand | 273 | 1 | 2 |
| α-helix | 287-301 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 134-138 | 5 | 3 |
| α-helix | 143-148 | 6 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 175-180 | 6 | |
| α-helix | 181-185 | 5 | |
| β-strand | 187-191 | 5 | 3 |
| α-helix | 206-222 | 17 | |
| β-strand | 226-230 | 5 | 3 |
| α-helix | 232-238 | 7 | |
| α-helix | 239-243 | 5 | |
| β-strand | 253-258 | 6 | 3 |
| β-strand | 265-269 | 5 | 3 |
| α-helix | 287-301 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| G/T mismatch-specific thymine DNA glycosylase | A, B | protein | 204 | Homo sapiens | Q13569 (AlphaFold model) |
| 5'-d(*cp*ap*gp*cp*tp*cp*tp*gp*tp*ap*cp*gp*tp*gp*ap*gp*cp*ap*gp*tp*gp*gp*a)-3' | C, E | DNA | 23 | ||
| 5'-D(*CP*CP*AP*CP*TP*GP*CP*TP*CP*AP*(UF2)P*GP*TP*AP*CP*AP*GP*AP*GP*CP*TP*GP*T)-3' | D, F | DNA | 23 |
>3UFJ_1 G/T mismatch-specific thymine DNA glycosylase (chains A, B) GSHMASFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLF MSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQP RIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQD KVHYYIKLKDLRDQLKGIERNMDV
>3UFJ_2 5'-D(*CP*AP*GP*CP*TP*CP*TP*GP*TP*AP*CP*GP*TP*GP*AP*GP*CP*AP*GP*TP*GP*GP*A)-3' (chains C, E) CAGCTCTGTACGTGAGCAGTGGA
>3UFJ_3 5'-D(*CP*CP*AP*CP*TP*GP*CP*TP*CP*AP*(UF2)P*GP*TP*AP*CP*AP*GP*AP*GP*CP*TP*GP*T)-3' (chains D, F) CCACTGCTCAXGTACAGAGCTGT
Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA. Maiti, A., Noon, M.S., Mackerell, A.D. et al. Proc Natl Acad Sci U S A (2012) 109:8091-8096. DOI 10.1073/pnas.1201010109 · PubMed
Other PDB entries of the same protein (UniProt Q13569 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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