3NS8: Ubiquitin

Crystal structure of an open conformation of Lys48-linked diubiquitin at pH 7.5. Determined by X-ray diffraction at 1.71 Å resolution. Released 20 Jul 2011.

Method
X-ray diffraction
Resolution
1.71 Å
Organism
Homo sapiens
Chains
2
Atoms
1,384
Mol. weight
17.58 kDa
Released
20 Jul 2011

Explore 3NS8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3NS8 contains 8 α-helices and 14 β-strands across 2 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.

Chains A and B: 4 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand2-651
β-strand12-1651
β-strand2212
α-helix23-3412
α-helix38-403
β-strand41-4551
β-strand48-4921
α-helix50-512
β-strand5512
α-helix56-594
β-strand66-7161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
UbiquitinA, Bprotein76Homo sapiensP62979 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3NS8_1 Ubiquitin (chains A, B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Primary citation

Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Lai, M.Y., Zhang, D., Laronde-Leblanc, N. et al. Biochim Biophys Acta (2012) 1823:2046-2056. DOI 10.1016/j.bbamcr.2012.04.003 · PubMed

Other PDB entries of the same protein (UniProt P62979 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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