The crystal structure of human Importin alpha 5 with TERT NLS peptide. Determined by X-ray diffraction at 2.52 Å resolution. Released 4 Sept 2013.
Explore 4B18 in 3D Show helices and sheets RCSB PDB PDBe
4B18 contains 35 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 | 85-91 | 7 | |
| α-helix | 96-111 | 16 | |
| α-helix | 118-122 | 5 | |
| α-helix | 127-134 | 8 | |
| α-helix | 141-154 | 14 | |
| α-helix | 159-167 | 9 | |
| α-helix | 170-177 | 8 | |
| α-helix | 183-197 | 15 | |
| α-helix | 201-209 | 9 | |
| α-helix | 213-218 | 6 | |
| α-helix | 219-221 | 3 | |
| α-helix | 226-240 | 15 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-252 | 4 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-262 | 7 | |
| α-helix | 268-281 | 14 | |
| α-helix | 286-294 | 9 | |
| α-helix | 298-304 | 7 | |
| α-helix | 310-323 | 14 | |
| α-helix | 328-336 | 9 | |
| α-helix | 339-346 | 8 | |
| α-helix | 352-365 | 14 | |
| α-helix | 370-378 | 9 | |
| α-helix | 381-391 | 11 | |
| α-helix | 394-410 | 17 | |
| α-helix | 413-422 | 10 | |
| α-helix | 425-430 | 6 | |
| α-helix | 431-433 | 3 | |
| α-helix | 437-460 | 24 | |
| α-helix | 467-474 | 8 | |
| α-helix | 477-483 | 7 | |
| α-helix | 484-486 | 3 | |
| α-helix | 490-503 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 238-240 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-1 | A | protein | 447 | HOMO SAPIENS | P52294 (AlphaFold model) |
| Telomerase reverse transcriptase | B | protein | 20 | HOMO SAPIENS | O14746 (AlphaFold model) |
>4B18_1 IMPORTIN SUBUNIT ALPHA-1 (chains A) GFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTP GVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDV QEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSP PPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELL MHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNI TAGNRAQIQTVIDANIFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCI KPLCDLLTVMDSKIVQVALNGLENILRLGEQEAKRNGTGINPYCALIEEAYGLDKIEFLQ SHENQEIYQKAFDLIEHYFGTEDEDSS
>4B18_2 TELOMERASE REVERSE TRANSCRIPTASE (chains B) RRRGGSASRSLPLPKRPRRA
Akt-Mediated Phosphorylation Increases the Binding Affinity of Htert for Importin Alpha to Promote Nuclear Translocation. Jeong, S.A., Kim, K., Lee, J.H. et al. J Cell Sci (2015) 128:2287. DOI 10.1242/JCS.166132 · PubMed
Other PDB entries of the same protein (UniProt P52294 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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