NMR Solution Structure of the Phi0 PKI NES Peptide in Complex with CRM1-RanGTP. Determined by solution NMR. Released 15 Jun 2011.
Explore 2L1L in 3D Show helices and sheets RCSB PDB PDBe
2L1L contains 10 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 | 7-14 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 510-530 | 21 | |
| α-helix | 534-550 | 17 | |
| α-helix | 552-557 | 6 | |
| α-helix | 559-572 | 14 | |
| α-helix | 580-594 | 15 | |
| α-helix | 596-599 | 4 | |
| α-helix | 602-603 | 2 | |
| α-helix | 610-615 | 6 | |
| α-helix | 618-622 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase inhibitor alpha | A | protein | 27 | Homo sapiens | P61925 (AlphaFold model) |
| Exportin-1 | B | protein | 127 | Homo sapiens | O14980 (AlphaFold model) |
>2L1L_1 cAMP-dependent protein kinase inhibitor alpha (chains A) GSASGNLNELALKLAGLDINKTEGEEC
>2L1L_2 Exportin-1 (chains B) ISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLK TVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIIC DLQPQQV
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Guttler, T., Madl, T., Neumann, P. et al. Nat Struct Mol Biol (2010) 17:1367-1376. DOI 10.1038/nsmb.1931 · PubMed
Other PDB entries of the same protein (UniProt P61925 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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