PDGFR beta-TM. Determined by solution NMR. Released 30 May 2012.
Explore 2L6W in 3D Show helices and sheets RCSB PDB PDBe
2L6W contains 2 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 | 6-32 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-33 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-type platelet-derived growth factor receptor | A, B | protein | 39 | Homo sapiens | P09619 (AlphaFold model) |
>2L6W_1 Beta-type platelet-derived growth factor receptor (chains A, B) GHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYE
Hydrophobic matching controls the tilt and stability of the dimeric platelet-derived growth factor receptor (PDGFR) beta transmembrane segment. Muhle-Goll, C., Hoffmann, S., Afonin, S. et al. J Biol Chem (2012) 287:26178-26186. DOI 10.1074/jbc.M111.325555 · PubMed
Other PDB entries of the same protein (UniProt P09619 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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