Putative active dimeric state of GHR transmembrane domain. Determined by solution NMR. Released 11 Apr 2018.
Explore 5OEK in 3D Show helices and sheets RCSB PDB PDBe
5OEK 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 | 266-292 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 267-290 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Growth hormone receptor | A, B | protein | 43 | Homo sapiens | P10912 (AlphaFold model) |
>5OEK_1 Growth hormone receptor (chains A, B) GSMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIK
Structural basis of the signal transduction via transmembrane domain of the human growth hormone receptor. Bocharov, E.V., Lesovoy, D.M., Bocharova, O.V. et al. Biochim Biophys Acta (2018) 1862:1410-1420. DOI 10.1016/j.bbagen.2018.03.022 · PubMed
Other PDB entries of the same protein (UniProt P10912 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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