5DPR: PLEKHM1 LIR-fused human LC3A_2-121

Crystal structure of PLEKHM1 LIR-fused human LC3A_2-121. Determined by X-ray diffraction at 2.5 Å resolution. Released 28 Sept 2016.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
4
Atoms
4,128
Mol. weight
63.73 kDa
Released
28 Sept 2016

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

Secondary structure: helices and β-sheets

5DPR contains 25 α-helices and 28 β-strands across 4 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, 7 β-strands

ElementResiduesLengthSheet
α-helix18-214
α-helix24-3714
β-strand41-4881
α-helix56-583
β-strand62-6651
β-strand7012
α-helix71-8111
β-strand91-9331
β-strand9811
β-strand10512
α-helix106-1138
α-helix1191
β-strand120-12561
Chain B: 6 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix18-214
α-helix24-3714
β-strand41-4883
α-helix56-583
β-strand62-6653
β-strand7014
α-helix71-8111
β-strand91-9443
β-strand9713
β-strand10514
α-helix106-1138
α-helix1191
β-strand120-12563
Chain C: 6 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix18-214
α-helix24-3714
β-strand41-4885
α-helix56-583
β-strand62-6655
β-strand7016
α-helix71-8212
β-strand91-9445
β-strand9715
β-strand10516
α-helix106-1138
α-helix1191
β-strand120-12565
Chain D: 7 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix18-214
α-helix24-3714
β-strand41-4887
α-helix56-583
β-strand62-6657
β-strand7018
α-helix71-8111
β-strand91-9337
β-strand9817
α-helix99-1013
β-strand10518
α-helix106-1138
α-helix1191
β-strand120-12567

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Pleckstrin homology domain-containing family M member 1,Microtubule-associated proteins 1A/1B…A, B, C, Dprotein136Homo sapiensQ9H492 (AlphaFold model), Q9Y4G2 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5DPR_1 Pleckstrin homology domain-containing family M member 1,Microtubule-associated proteins 1A/1B light chain 3A (chains A, B, C, D)
GSVRPQQEDEWVNVGSPSDRPFKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLP
VLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTPIADIYEQEKDE
DGFLYMVYASQETFGF

Primary citation

Structural and functional analysis of the GABARAP interaction motif (GIM). Rogov, V.V., Stolz, A., Ravichandran, A.C. et al. EMBO Rep (2017) 18:1382-1396. DOI 10.15252/embr.201643587 · PubMed

Other PDB entries of the same protein (UniProt Q9H492 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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