1AKZ: Human uracil-DNA glycosylase

Human uracil-DNA glycosylase. Determined by X-ray diffraction at 1.57 Å resolution. Released 20 Aug 1997.

Method
X-ray diffraction
Resolution
1.57 Å
Organism
Homo sapiens
Chains
1
Atoms
1,993
Mol. weight
25.54 kDa
Released
20 Aug 1997

Explore 1AKZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 14 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix87-9711
α-helix100-11516
β-strand118-11921
α-helix122-1243
α-helix127-1293
α-helix134-1363
β-strand139-14352
α-helix165-1673
α-helix168-18013
α-helix193-1975
β-strand200-20452
β-strand209-21021
β-strand21311
α-helix222-23615
β-strand241-24552
α-helix247-2526
α-helix253-2553
β-strand262-26652
α-helix274-2763
α-helix283-29311
α-helix297-2993

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Uracil-DNA glycosylaseAprotein223Homo sapiensP13051 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1AKZ_1 URACIL-DNA GLYCOSYLASE (chains A)
MEFFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVI
LGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVL
LLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRH
HVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL

Primary citation

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:

Browse structure collections

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