4BSN: Exportin-1

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.

Method
X-ray diffraction
Resolution
4.1 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
5,481
Mol. weight
118.86 kDa
Released
31 Jul 2013

Explore 4BSN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 42 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix4-1815
α-helix24-3613
α-helix38-5215
α-helix58-647
α-helix73-9018
α-helix96-11419
α-helix118-1214
α-helix125-14117
α-helix149-1568
α-helix161-17414
α-helix188-21528
α-helix219-23113
α-helix238-2403
α-helix246-2527
α-helix261-27212
α-helix275-2762
α-helix281-29717
α-helix304-3096
α-helix313-33927
α-helix343-35715
α-helix363-38321
α-helix404-42320
β-strand433-43421
β-strand440-44121
α-helix449-46719
α-helix469-48517
α-helix491-50414
α-helix510-53021
α-helix533-54917
α-helix552-5554
α-helix559-57214
α-helix580-59415
α-helix596-6005
α-helix610-62112
α-helix627-64115
α-helix648-66619
α-helix692-70211
α-helix707-7104
α-helix714-7229
α-helix759-7657
α-helix769-7713
α-helix772-7765
α-helix781-7855
α-helix786-7894

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Exportin-1Aprotein1032HOMO SAPIENSO14980 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4BSN_1 EXPORTIN-1 (chains A)
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAW
TRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCV
EKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFD
FSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGY
IFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPL
NTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEV
EETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLM
VSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKL
HNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAII
ASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFV
QVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLL
PNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNV
YKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPL
LDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEE
YPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTL
LQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKIST
SLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLV
QIKEFAGEDTSD

Primary citation

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:

Browse structure collections

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