Escherichia coli uracil-DNA glycosylase:inhibitor complex with wild-type udg and wild-type ugi. Determined by X-ray diffraction at 2.4 Å resolution. Released 25 Mar 1999.
Explore 1UUG in 3D Show helices and sheets RCSB PDB PDBe
1UUG contains 32 α-helices and 24 β-strands across 4 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 | 7-11 | 5 | |
| α-helix | 14-16 | 3 | |
| α-helix | 18-32 | 15 | |
| β-strand | 37-38 | 2 | 1 |
| α-helix | 41-43 | 3 | |
| α-helix | 46-50 | 5 | |
| α-helix | 53-55 | 3 | |
| β-strand | 58-62 | 5 | 2 |
| α-helix | 84-86 | 3 | |
| α-helix | 87-97 | 11 | |
| α-helix | 112-115 | 4 | |
| β-strand | 119-123 | 5 | 2 |
| β-strand | 128-129 | 2 | 1 |
| β-strand | 132 | 1 | 1 |
| α-helix | 141-155 | 15 | |
| β-strand | 160-164 | 5 | 2 |
| α-helix | 166-171 | 6 | |
| β-strand | 181-185 | 5 | 2 |
| α-helix | 193-195 | 3 | |
| α-helix | 202-212 | 11 | |
| α-helix | 216-218 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-12 | 9 | |
| β-strand | 20-24 | 5 | 3 |
| α-helix | 26-33 | 8 | |
| β-strand | 41-48 | 8 | 3 |
| β-strand | 53-60 | 8 | 3 |
| β-strand | 67-73 | 7 | 3 |
| β-strand | 79-83 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-11 | 5 | |
| α-helix | 14-16 | 3 | |
| α-helix | 18-32 | 15 | |
| β-strand | 37-38 | 2 | 4 |
| α-helix | 46-50 | 5 | |
| α-helix | 53-55 | 3 | |
| β-strand | 58-62 | 5 | 5 |
| α-helix | 84-86 | 3 | |
| α-helix | 87-99 | 13 | |
| α-helix | 112-116 | 5 | |
| β-strand | 119-123 | 5 | 5 |
| β-strand | 128-129 | 2 | 4 |
| β-strand | 132 | 1 | 4 |
| α-helix | 141-155 | 15 | |
| β-strand | 160-164 | 5 | 5 |
| α-helix | 166-169 | 4 | |
| α-helix | 170-173 | 4 | |
| β-strand | 181-185 | 5 | 5 |
| α-helix | 193-195 | 3 | |
| α-helix | 202-212 | 11 | |
| α-helix | 216-218 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Uracil-DNA glycosylase | A, C | protein | 229 | Escherichia coli K12 | P12295 (AlphaFold model) |
| Uracil-DNA glycosylase inhibitor | B, D | protein | 84 | Bacillus phage PBS2 | P14739 (AlphaFold model) |
>1UUG_1 URACIL-DNA GLYCOSYLASE (chains A, C) MANELTWHDVLAEEKQQPYFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVI LGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVL LLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRH HVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQRGETPIDWMPVLPAESE
>1UUG_2 URACIL-DNA GLYCOSYLASE INHIBITOR (chains B, D) MTNLSDIIEKETGKQLVIQESILMLPEEVEEVIGNKPESDILVHTAYDESTDENVMLLTS DAPEYKPWALVIQDSNGENKIKML
Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase. Putnam, C.D., Shroyer, M.J., Lundquist, A.J. et al. J Mol Biol (1999) 287:331-346. DOI 10.1006/jmbi.1999.2605 · PubMed
Other PDB entries of the same protein (UniProt P12295 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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