Coiled-coil structure of liprin-alpha2_H2delC. Determined by X-ray diffraction at 1.7 Å resolution. Released 7 Apr 2021.
Explore 7D2G in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 102-147 | 46 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 98-145 | 48 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 100-144 | 45 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Liprin-alpha-2 | A, B, C, D | protein | 55 | Homo sapiens | O75334 (AlphaFold model) |
>7D2G_1 Liprin-alpha-2 (chains A, B, C, D) GPGSEFEFAAMTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEALVSRHER
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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