1AAR: Di-ubiquitin

Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2). Determined by X-ray diffraction at 2.3 Å resolution. Released 31 Oct 1993.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Bos taurus
Chains
2
Atoms
1,218
Mol. weight
17.15 kDa
Released
31 Oct 1993

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

Secondary structure: helices and β-sheets

1AAR contains 7 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.

Chain A: 3 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand2-761
β-strand12-1651
β-strand2212
α-helix23-3412
α-helix38-403
β-strand41-4551
β-strand48-4921
α-helix50-512
β-strand5512
β-strand66-7161
Chain B: 4 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand2-761
β-strand12-1651
β-strand2213
α-helix23-3412
α-helix38-403
β-strand41-4551
β-strand48-4921
α-helix50-512
β-strand5513
α-helix57-593
β-strand66-7161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Di-ubiquitinA, Bprotein76Bos taurusP0CH28 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1AAR_1 DI-UBIQUITIN (chains A, B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Primary citation

Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2). Cook, W.J., Jeffrey, L.C., Carson, M. et al. J Biol Chem (1992) 267:16467-16471. PubMed

Other PDB entries of the same protein (UniProt P0CH28 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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