1Z3H: Importin alpha re-exporter

The exportin Cse1 in its cargo-free, cytoplasmic state. Determined by X-ray diffraction at 3.1 Å resolution. Released 10 May 2005.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
14,787
Mol. weight
221.08 kDa
Ligands
MG
Released
10 May 2005

Explore 1Z3H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Z3H contains 135 α-helices and 12 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.

Chain A: 69 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix3-1412
α-helix17-193
α-helix20-3112
α-helix36-4510
α-helix51-6818
β-strand7011
β-strand7611
α-helix80-9617
α-helix99-11618
α-helix123-1297
α-helix137-15115
α-helix163-19129
α-helix196-21722
α-helix223-2275
α-helix229-24113
α-helix245-2473
α-helix258-27619
α-helix278-29619
α-helix303-3053
α-helix306-32015
α-helix323-3264
α-helix332-3387
α-helix339-3435
α-helix344-3474
α-helix351-3599
α-helix361-3688
α-helix377-41337
α-helix420-43314
β-strand43412
β-strand44612
α-helix452-4554
α-helix456-4605
α-helix462-4654
α-helix472-48514
α-helix486-4883
α-helix491-4955
α-helix498-5047
α-helix510-52819
α-helix544-55815
α-helix564-5674
α-helix571-58111
α-helix589-5913
α-helix592-60716
α-helix613-62917
α-helix632-6343
α-helix635-65117
α-helix658-67114
α-helix680-6834
α-helix684-6874
α-helix689-6935
α-helix695-6973
α-helix698-71114
α-helix713-7153
α-helix720-73011
α-helix733-7353
α-helix736-74914
α-helix752-7543
α-helix759-77315
α-helix776-79318
α-helix795-8039
α-helix809-8135
α-helix814-8185
α-helix819-8213
α-helix822-8243
α-helix828-84316
α-helix848-8514
α-helix853-86816
α-helix894-8963
α-helix899-9013
β-strand91313
β-strand916-91723
α-helix918-93013
α-helix937-9415
α-helix942-9443
α-helix947-95812
Chain B: 66 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix3-1513
α-helix17-193
α-helix20-3112
α-helix36-4510
α-helix51-6818
β-strand7014
β-strand7614
α-helix80-9617
α-helix99-11517
α-helix123-1308
α-helix137-15115
α-helix152-1543
α-helix163-19129
α-helix196-21621
α-helix223-2275
α-helix229-24113
α-helix245-2473
α-helix258-27518
α-helix282-29615
α-helix303-3053
α-helix306-32015
α-helix323-3264
α-helix334-3374
α-helix338-3436
α-helix344-3474
α-helix349-3502
α-helix351-3599
α-helix361-3688
α-helix377-41337
α-helix419-43315
β-strand43415
β-strand43916
β-strand44216
β-strand44615
α-helix452-4554
α-helix456-4605
α-helix462-4643
α-helix472-48514
α-helix491-50414
α-helix510-52415
α-helix546-55813
α-helix567-5693
α-helix571-58313
α-helix589-5913
α-helix593-60715
α-helix613-62917
α-helix636-64914
α-helix658-67013
α-helix680-6823
α-helix683-6864
α-helix691-6933
α-helix698-71013
α-helix713-7153
α-helix719-73113
α-helix736-74813
α-helix752-7554
α-helix756-7583
α-helix759-77214
α-helix776-79318
α-helix795-8039
α-helix810-8134
α-helix814-8185
α-helix819-8213
α-helix822-8243
α-helix828-84215
α-helix854-86714
α-helix907-9093
α-helix919-92810
α-helix930-9334
α-helix937-9415
α-helix942-9443
α-helix947-95812

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Importin alpha re-exporterA, Bprotein968Saccharomyces cerevisiaeP33307 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1Z3H_1 Importin alpha re-exporter (chains A, B)
MSDLETVAKFLAESVIASTAKTSERNLRQLETQDGFGLTLLHVIASTNLPLSTRLAGALF
FKNFIKRKWVDENGNHLLPANNVELIKKEIVPLMISLPNNLQVQIGEAISSIADSDFPDR
WPTLLSDLASRLSNDDMVTNKGVLTVAHSIFKRWRPLFRSDELFLEIKLVLDVFTAPFLN
LLKTVDEQITANENNKASLNILFDVLLVLIKLYYDFNCQDIPEFFEDNIQVGMGIFHKYL
SYSNPLLEDPDETEHASVLIKVKSSIQELVQLYTTRYEDVFGPMINEFIQITWNLLTSIS
NQPKYDILVSKSLSFLTAVTRIPKYFEIFNNESAMNNITEQIILPNVTLREEDVELFEDD
PIEYIRRDLEGSDTDTRRRACTDFLKELKEKNEVLVTNIFLAHMKGFVDQYMSDPSKNWK
FKDLYIYLFTALAINGNITNAGVSSTNNLLNVVDFFTKEIAPDLTSNNIPHIILRVDAIK
YIYTFRNQLTKAQLIELMPILATFLQTDEYVVYTYAAITIEKILTIRESNTSPAFIFHKE
DISNSTEILLKNLIALILKHGSSPEKLAENEFLMRSIFRVLQTSEDSIQPLFPQLLAQFI
EIVTIMAKNPSNPRFTHYTFESIGAILNYTQRQNLPLLVDSMMPTFLTVFSEDIQEFIPY
VFQIIAFVVEQSATIPESIKPLAQPLLAPNVWELKGNIPAVTRLLKSFIKTDSSIFPDLV
PVLGIFQRLIASKAYEVHGFDLLEHIMLLIDMNRLRPYIKQIAVLLLQRLQNSKTERYVK
KLTVFFGLISNKLGSDFLIHFIDEVQDGLFQQIWGNFIITTLPTIGNLLDRKIALIGVLN
MVINGQFFQSKYPTLISSTMNSIIETASSQSIANLKNDYVDLDNLEEISTFGSHFSKLVS
ISEKPFDPLPEIDVNNGVRLYVAEALNKYNAISGNTFLNTILPQLTQENQVKLNQLLVGN
RSHHHHHH

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Primary citation

The structure of the nuclear export receptor cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Cook, A., Fernandez, E., Lindner, D. et al. Mol Cell (2005) 18:355-367. DOI 10.1016/j.molcel.2005.03.021 · PubMed

Other PDB entries of the same protein (UniProt P33307 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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