Crystallographic and enzymatic studies of an active site variant H187Q of escherichia coli uracil DNA glycosylase: crystal structures of mutant H187Q and its uracil complex. Determined by X-ray diffraction at 1.6 Å resolution. Released 23 Jul 1999.
Explore 5EUG in 3D Show helices and sheets RCSB PDB PDBe
5EUG contains 16 α-helices and 7 β-strands across 1 chain. 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 | 65-66 | 2 | |
| α-helix | 84-86 | 3 | |
| α-helix | 87-99 | 13 | |
| α-helix | 112-116 | 5 | |
| 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 | 215-218 | 4 | |
| α-helix | 224-227 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (glycosylase) | A | protein | 229 | Escherichia coli | P12295 (AlphaFold model) |
>5EUG_1 PROTEIN (GLYCOSYLASE) (chains A) MANELTWHDVLAEEKQQPYFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVI LGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVL LLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRH HVLKAPQPSPLSAHRGFFGCNHFVLANQWLEQHGETPIDWMPVLPAESE
| ID | Name | Formula | Copies |
|---|---|---|---|
| URA | Uracil | C4 H4 N2 O2 | 1 |
Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited. Xiao, G., Tordova, M., Jagadeesh, J. et al. Proteins (1999) 35:13-24. DOI 10.1002/(SICI)1097-0134(19990401)35:1<13::AID-PROT2>3.3.CO;2-U · 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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