Lem domain of human inner nuclear membrane protein emerin. Determined by solution NMR. Released 4 Jul 2001.
Explore 1JEI in 3D Show helices and sheets RCSB PDB PDBe
1JEI contains 3 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 8-15 | 8 | |
| α-helix | 28-30 | 3 | |
| α-helix | 31-39 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Emerin | A | protein | 53 | P50402 (AlphaFold model) |
>1JEI_1 EMERIN (chains A) DNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSS
Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy. Wolff, N., Gilquin, B., Courchay, K. et al. FEBS Lett (2001) 501:171-176. DOI 10.1016/S0014-5793(01)02649-7 · PubMed
Other PDB entries of the same protein (UniProt P50402 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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