8X8A: STBD1 LIR motif

Crystal structure of STBD1 LIR motif in complex with GABARAPL1. Determined by X-ray diffraction at 1.53 Å resolution. Released 18 Sept 2024.

Method
X-ray diffraction
Resolution
1.53 Å
Organism
Homo sapiens
Chains
2
Atoms
1,285
Mol. weight
16.09 kDa
Released
18 Sept 2024

Explore 8X8A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8X8A contains 8 α-helices and 9 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: 6 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix4-85
α-helix11-2414
β-strand28-3581
α-helix361
β-strand48-5251
β-strand5612
α-helix57-6711
β-strand77-7931
β-strand8013
β-strand8313
α-helix84-863
β-strand9012
α-helix91-988
β-strand105-11061
Chain B: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix202-2032
β-strand204-20521
α-helix206-2072

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Gamma-aminobutyric acid receptor-associated protein-like 1Aprotein117Homo sapiensQ9H0R8 (AlphaFold model)
Starch-binding domain-containing protein 1Bprotein19Homo sapiensO95210 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8X8A_1 Gamma-aminobutyric acid receptor-associated protein-like 1 (chains A)
MKFQYKEDHPFEYRKKEGEKIRKKYPDRVPVIVEKAPKARVPDLDKRKYLVPSDLTVGQF
YFLIRKRIHLRPEDALFFFVNNTIPPTSATMGQLYEDNHEEDYFLYVAYSDESVYGK
Sequence of entity 2 (B), FASTA
>8X8A_2 Starch-binding domain-containing protein 1 (chains B)
GPGSHEEWEMVPRHSGSGS

Primary citation

Decoding the molecular mechanism of selective autophagy of glycogen mediated by autophagy receptor STBD1. Zhang, Y., Sun, Y., Shi, J. et al. Proc Natl Acad Sci U S A (2024) 121:e2402817121-e2402817121. DOI 10.1073/pnas.2402817121 · PubMed

Other PDB entries of the same protein (UniProt Q9H0R8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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