7D2G: Coiled-coil structure of liprin-alpha2_H2delC

Coiled-coil structure of liprin-alpha2_H2delC. Determined by X-ray diffraction at 1.7 Å resolution. Released 7 Apr 2021.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
4
Atoms
1,743
Mol. weight
25.9 kDa
Released
7 Apr 2021

Explore 7D2G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7D2G contains 4 α-helices and 0 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: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix102-14746
Chains B and D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix98-14548
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix100-14445

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Liprin-alpha-2A, B, C, Dprotein55Homo sapiensO75334 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7D2G_1 Liprin-alpha-2 (chains A, B, C, D)
GPGSEFEFAAMTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEALVSRHER

Primary citation

Oligomerized liprin-alpha promotes phase separation of ELKS for compartmentalization of presynaptic active zone proteins. Liang, M., Jin, G., Xie, X. et al. Cell Rep (2021) 34:108901-108901. DOI 10.1016/j.celrep.2021.108901 · PubMed

Other PDB entries of the same protein (UniProt O75334 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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