Escherichia coli uracil-DNA glycosylase. Determined by X-ray diffraction at 3.35 Å resolution. Released 10 Nov 2002.
Explore 1LQJ in 3D Show helices and sheets RCSB PDB PDBe
1LQJ contains 49 α-helices and 29 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 | 37-38 | 2 | 1 |
| α-helix | 41-44 | 4 | |
| α-helix | 46-50 | 5 | |
| α-helix | 53-55 | 3 | |
| β-strand | 58-62 | 5 | 2 |
| α-helix | 87-99 | 13 | |
| α-helix | 112-115 | 4 | |
| β-strand | 119-123 | 5 | 2 |
| β-strand | 128-129 | 2 | 1 |
| β-strand | 132 | 1 | 1 |
| α-helix | 141-154 | 14 | |
| β-strand | 160-164 | 5 | 2 |
| α-helix | 166-171 | 6 | |
| β-strand | 181-185 | 5 | 2 |
| α-helix | 202-212 | 11 | |
| α-helix | 215-218 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 14-16 | 3 | |
| α-helix | 19-32 | 14 | |
| β-strand | 37-38 | 2 | 3 |
| α-helix | 46-50 | 5 | |
| α-helix | 53-55 | 3 | |
| β-strand | 58-62 | 5 | 4 |
| α-helix | 87-99 | 13 | |
| α-helix | 112-115 | 4 | |
| β-strand | 119-123 | 5 | 4 |
| β-strand | 128-129 | 2 | 3 |
| β-strand | 132 | 1 | 3 |
| α-helix | 141-155 | 15 | |
| β-strand | 160-164 | 5 | 4 |
| α-helix | 168-171 | 4 | |
| α-helix | 172-174 | 3 | |
| β-strand | 181-185 | 5 | 4 |
| α-helix | 193-195 | 3 | |
| α-helix | 202-212 | 11 | |
| α-helix | 216-218 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 14-16 | 3 | |
| α-helix | 18-32 | 15 | |
| β-strand | 37-38 | 2 | 5 |
| α-helix | 46-50 | 5 | |
| α-helix | 53-55 | 3 | |
| β-strand | 58-62 | 5 | 6 |
| β-strand | 72 | 1 | 7 |
| α-helix | 78 | 1 | |
| β-strand | 79 | 1 | 7 |
| α-helix | 80 | 1 | |
| α-helix | 84-86 | 3 | |
| α-helix | 87-98 | 12 | |
| α-helix | 115-117 | 3 | |
| β-strand | 119-123 | 5 | 6 |
| β-strand | 128-129 | 2 | 5 |
| α-helix | 141-154 | 14 | |
| β-strand | 160-164 | 5 | 6 |
| α-helix | 165-171 | 7 | |
| β-strand | 181-185 | 5 | 6 |
| α-helix | 193-195 | 3 | |
| α-helix | 202-212 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 14-16 | 3 | |
| α-helix | 18-32 | 15 | |
| β-strand | 37-38 | 2 | 8 |
| α-helix | 41-43 | 3 | |
| α-helix | 46-50 | 5 | |
| β-strand | 58-62 | 5 | 9 |
| α-helix | 79-80 | 2 | |
| α-helix | 87-99 | 13 | |
| α-helix | 112-115 | 4 | |
| β-strand | 119-123 | 5 | 9 |
| β-strand | 128-129 | 2 | 8 |
| β-strand | 132 | 1 | 8 |
| α-helix | 141-155 | 15 | |
| β-strand | 160-164 | 5 | 9 |
| α-helix | 165-172 | 8 | |
| β-strand | 181-185 | 5 | 9 |
| α-helix | 193-195 | 3 | |
| α-helix | 202-212 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Uracil-DNA glycosylase | A, B, C, D | protein | 229 | Escherichia coli | P12295 (AlphaFold model) |
>1LQJ_1 URACIL-DNA GLYCOSYLASE (chains A, B, C, D) MANELTWHDVLAEEKQQPYFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVI LGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVL LLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRH HVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQRGETPIDWMPVLPAESE
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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