Escherichia coli uracil-DNA glycosylase complex with uracil-DNA glycosylase inhibitor protein. Determined by X-ray diffraction at 2.9 Å resolution. Released 10 Nov 2002.
Explore 1LQG in 3D Show helices and sheets RCSB PDB PDBe
1LQG contains 24 α-helices and 26 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 | 18-33 | 16 | |
| β-strand | 37 | 1 | 1 |
| α-helix | 46-50 | 5 | |
| α-helix | 53-55 | 3 | |
| β-strand | 58-62 | 5 | 2 |
| α-helix | 84-86 | 3 | |
| α-helix | 87-99 | 13 | |
| α-helix | 112-115 | 4 | |
| β-strand | 119-123 | 5 | 2 |
| β-strand | 129 | 1 | 1 |
| β-strand | 132 | 1 | 1 |
| α-helix | 141-155 | 15 | |
| β-strand | 160-164 | 5 | 2 |
| α-helix | 165-168 | 4 | |
| β-strand | 181-185 | 5 | 2 |
| α-helix | 190-192 | 3 | |
| α-helix | 193-197 | 5 | |
| α-helix | 202-213 | 12 | |
| α-helix | 215-218 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-14 | 4 | |
| α-helix | 18-33 | 16 | |
| β-strand | 37 | 1 | 3 |
| α-helix | 46-50 | 5 | |
| α-helix | 53-55 | 3 | |
| β-strand | 58-62 | 5 | 4 |
| β-strand | 72 | 1 | 5 |
| β-strand | 79 | 1 | 5 |
| α-helix | 87-99 | 13 | |
| α-helix | 112-115 | 4 | |
| β-strand | 119-123 | 5 | 4 |
| β-strand | 129 | 1 | 3 |
| β-strand | 132 | 1 | 3 |
| α-helix | 141-155 | 15 | |
| β-strand | 160-164 | 5 | 4 |
| α-helix | 165-166 | 2 | |
| α-helix | 167-171 | 5 | |
| β-strand | 181-185 | 5 | 4 |
| α-helix | 202-212 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20-24 | 5 | 6 |
| α-helix | 26-33 | 8 | |
| β-strand | 41-46 | 6 | 6 |
| β-strand | 54-60 | 7 | 6 |
| β-strand | 67-73 | 7 | 6 |
| β-strand | 79-83 | 5 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20-24 | 5 | 7 |
| α-helix | 26-33 | 8 | |
| β-strand | 41-48 | 8 | 7 |
| β-strand | 53-60 | 8 | 7 |
| β-strand | 67-73 | 7 | 7 |
| β-strand | 79-83 | 5 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Uracil-DNA glycosylase | A, B | protein | 229 | Escherichia coli | P12295 (AlphaFold model) |
| Uracil-DNA glycosylase inhibitor | C, D | protein | 84 | Bacillus phage PBS2 | P14739 (AlphaFold model) |
>1LQG_1 URACIL-DNA GLYCOSYLASE (chains A, B) MANELTWHDVLAEEKQQPYFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVI LGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVL LLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRH HVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQRGETPIDWMPVLPAESE
>1LQG_2 URACIL-DNA GLYCOSYLASE INHIBITOR (chains C, D) MTNLSDIIEKETGKQLVIQESILMLPEEVEEVIGNKPESDILVHTAYDESTDENVMLLTS DAPEYKPWALVIQDSNGENKIKML
Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG. Saikrishnan, K., Bidya Sagar, M., Ravishankar, R. et al. Acta Crystallogr D Biol Crystallogr (2002) 58:1269-1276. DOI 10.1107/S0907444902009599 · 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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