Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.1A. Determined by X-ray diffraction at 4.1 Å resolution. Released 31 Jul 2013.
Explore 4BSN in 3D Show helices and sheets RCSB PDB PDBe
4BSN contains 42 α-helices and 2 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 | 4-18 | 15 | |
| α-helix | 24-36 | 13 | |
| α-helix | 38-52 | 15 | |
| α-helix | 58-64 | 7 | |
| α-helix | 73-90 | 18 | |
| α-helix | 96-114 | 19 | |
| α-helix | 118-121 | 4 | |
| α-helix | 125-141 | 17 | |
| α-helix | 149-156 | 8 | |
| α-helix | 161-174 | 14 | |
| α-helix | 188-215 | 28 | |
| α-helix | 219-231 | 13 | |
| α-helix | 238-240 | 3 | |
| α-helix | 246-252 | 7 | |
| α-helix | 261-272 | 12 | |
| α-helix | 275-276 | 2 | |
| α-helix | 281-297 | 17 | |
| α-helix | 304-309 | 6 | |
| α-helix | 313-339 | 27 | |
| α-helix | 343-357 | 15 | |
| α-helix | 363-383 | 21 | |
| α-helix | 404-423 | 20 | |
| β-strand | 433-434 | 2 | 1 |
| β-strand | 440-441 | 2 | 1 |
| α-helix | 449-467 | 19 | |
| α-helix | 469-485 | 17 | |
| α-helix | 491-504 | 14 | |
| α-helix | 510-530 | 21 | |
| α-helix | 533-549 | 17 | |
| α-helix | 552-555 | 4 | |
| α-helix | 559-572 | 14 | |
| α-helix | 580-594 | 15 | |
| α-helix | 596-600 | 5 | |
| α-helix | 610-621 | 12 | |
| α-helix | 627-641 | 15 | |
| α-helix | 648-666 | 19 | |
| α-helix | 692-702 | 11 | |
| α-helix | 707-710 | 4 | |
| α-helix | 714-722 | 9 | |
| α-helix | 759-765 | 7 | |
| α-helix | 769-771 | 3 | |
| α-helix | 772-776 | 5 | |
| α-helix | 781-785 | 5 | |
| α-helix | 786-789 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Exportin-1 | A | protein | 1032 | HOMO SAPIENS | O14980 (AlphaFold model) |
>4BSN_1 EXPORTIN-1 (chains A) MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAW TRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCV EKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFD FSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGY IFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPL NTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEV EETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLM VSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKL HNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAII ASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFV QVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLL PNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNV YKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPL LDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEE YPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTL LQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKIST SLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLV QIKEFAGEDTSD
Structure of a Truncation Mutant of the Nuclear Export Factor Crm1 Provides Insights Into the Auto-Inhibitory Role of its C-Terminal Helix. Dian, C., Bernaudat, F., Langer, K. et al. Structure (2013) 21:1338. DOI 10.1016/J.STR.2013.06.003 · PubMed
Other PDB entries of the same protein (UniProt O14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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