FLRT2 LRR domain. Determined by X-ray diffraction at 2.5 Å resolution. Released 5 Nov 2014.
Explore 4V2D in 3D Show helices and sheets RCSB PDB PDBe
4V2D contains 9 α-helices and 26 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 41-43 | 3 | 1 |
| β-strand | 46-48 | 3 | 1 |
| β-strand | 67-69 | 3 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 92-94 | 3 | 1 |
| β-strand | 102 | 1 | 2 |
| α-helix | 103-104 | 2 | |
| β-strand | 113-115 | 3 | 1 |
| β-strand | 123 | 1 | 2 |
| β-strand | 124 | 1 | 3 |
| α-helix | 126-131 | 6 | |
| β-strand | 137-139 | 3 | 1 |
| β-strand | 150 | 1 | 3 |
| α-helix | 155-157 | 3 | |
| β-strand | 163-165 | 3 | 1 |
| β-strand | 173 | 1 | 4 |
| β-strand | 184-186 | 3 | 1 |
| β-strand | 194 | 1 | 4 |
| β-strand | 195 | 1 | 5 |
| β-strand | 208-210 | 3 | 1 |
| β-strand | 221 | 1 | 5 |
| α-helix | 222 | 1 | |
| β-strand | 234-236 | 3 | 1 |
| α-helix | 245-246 | 2 | |
| β-strand | 256-258 | 3 | 1 |
| β-strand | 280-282 | 3 | 1 |
| β-strand | 304-306 | 3 | 1 |
| β-strand | 312-313 | 2 | 6 |
| α-helix | 316-318 | 3 | |
| α-helix | 319-327 | 9 | |
| β-strand | 333-335 | 3 | 1 |
| β-strand | 338 | 1 | 7 |
| β-strand | 339-341 | 3 | 6 |
| β-strand | 349 | 1 | 7 |
| α-helix | 350-352 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibronectin leucine rich transmembrane protein 2 | A | protein | 326 | HOMO SAPIENS | Q8BLU0 (AlphaFold model) |
>4V2D_1 FIBRONECTIN LEUCINE RICH TRANSMEMBRANE PROTEIN 2 (chains A) CPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYL YGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAF REAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNL LTNKGIAEGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANL RKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCDCSIKWVTEWLKYIPSSLNVR GFMCQGPEQVRGMAVRALNMNLLSCP
Flrt Structure: Balancing Repulsion and Cell Adhesion in Cortical and Vascular Development. Seiradake, E., Del Toro, D., Nagel, D. et al. Neuron (2014) 84:370. DOI 10.1016/J.NEURON.2014.10.008 · PubMed
Other PDB entries of the same protein (UniProt Q8BLU0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4V2D directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.