5YR0: Beclin1-UVRAG coiled coil domain complex

Structure of Beclin1-UVRAG coiled coil domain complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 13 Jun 2018.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Mus musculus
Chains
2
Atoms
999
Mol. weight
11.59 kDa
Released
13 Jun 2018

Explore 5YR0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5YR0 contains 2 α-helices and 0 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: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix176-22146
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix232-27342

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Beclin-1Aprotein50Mus musculusO88597 (AlphaFold model)
UV radiation resistance associated proteinBprotein48Mus musculusQ8K245 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5YR0_1 Beclin-1 (chains A)
DSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQE
Sequence of entity 2 (B), FASTA
>5YR0_2 UV radiation resistance associated protein (chains B)
TSNELKKESESLRLKILVLRNELERQKKALGREVAFLHKQQMALQDKG

Primary citation

Targeting the potent Beclin 1-UVRAG coiled-coil interaction with designed peptides enhances autophagy and endolysosomal trafficking. Wu, S., He, Y., Qiu, X. et al. Proc Natl Acad Sci U S A (2018) 115:E5669-E5678. DOI 10.1073/pnas.1721173115 · PubMed

Other PDB entries of the same protein (UniProt O88597 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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