Human uracil-DNA glycosylase. Determined by X-ray diffraction at 1.57 Å resolution. Released 20 Aug 1997.
Explore 1AKZ in 3D Show helices and sheets RCSB PDB PDBe
1AKZ contains 14 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 | 87-97 | 11 | |
| α-helix | 100-115 | 16 | |
| β-strand | 118-119 | 2 | 1 |
| α-helix | 122-124 | 3 | |
| α-helix | 127-129 | 3 | |
| α-helix | 134-136 | 3 | |
| β-strand | 139-143 | 5 | 2 |
| α-helix | 165-167 | 3 | |
| α-helix | 168-180 | 13 | |
| α-helix | 193-197 | 5 | |
| β-strand | 200-204 | 5 | 2 |
| β-strand | 209-210 | 2 | 1 |
| β-strand | 213 | 1 | 1 |
| α-helix | 222-236 | 15 | |
| β-strand | 241-245 | 5 | 2 |
| α-helix | 247-252 | 6 | |
| α-helix | 253-255 | 3 | |
| β-strand | 262-266 | 5 | 2 |
| α-helix | 274-276 | 3 | |
| α-helix | 283-293 | 11 | |
| α-helix | 297-299 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Uracil-DNA glycosylase | A | protein | 223 | Homo sapiens | P13051 (AlphaFold model) |
>1AKZ_1 URACIL-DNA GLYCOSYLASE (chains A) MEFFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVI LGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVL LLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRH HVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL
Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. Parikh, S.S., Mol, C.D., Slupphaug, G. et al. EMBO J (1998) 17:5214-5226. DOI 10.1093/emboj/17.17.5214 · PubMed
Other PDB entries of the same protein (UniProt P13051 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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