Crystal structure of the ELKS2/LL5beta complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Aug 2024.
Explore 8WHM in 3D Show helices and sheets RCSB PDB PDBe
8WHM contains 3 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 262-312 | 51 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 422-461 | 40 | |
| α-helix | 473-486 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ERC protein 2 | A | protein | 66 | Rattus norvegicus | Q8K3M6 (AlphaFold model) |
| Pleckstrin homology-like domain family B member 2 | B | protein | 82 | Homo sapiens | Q86SQ0 (AlphaFold model) |
>8WHM_1 ERC protein 2 (chains A) GPGSEFLTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEM LQSKGL
>8WHM_2 Pleckstrin homology-like domain family B member 2 (chains B) GPGSKSSISSISGRDDLMDYHRRQREERLREQEMERLERQRLETILSLCAEYTKPDSRLS TGTTVEDVQKINKELEKLQLSD
CLASP-mediated competitive binding in protein condensates directs microtubule growth. Jia, X., Lin, L., Guo, S. et al. Nat Commun (2024) 15:6509-6509. DOI 10.1038/s41467-024-50863-3 · PubMed
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