1EE4: Karyopherin alpha

Crystal structure of yeast karyopherin (importin) alpha in a complex with a C-myc nls peptide. Determined by X-ray diffraction at 2.1 Å resolution. Released 29 Mar 2000.

Method
X-ray diffraction
Resolution
2.1 Å
Organisms
Saccharomyces cerevisiae, Homo sapiens
Chains
6
Atoms
6,817
Mol. weight
97.74 kDa
Released
29 Mar 2000

Explore 1EE4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EE4 contains 68 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.

Chain A: 33 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix89-968
α-helix101-11515
α-helix123-1286
α-helix132-1376
α-helix145-15814
α-helix163-1719
α-helix174-18411
α-helix187-20115
α-helix205-2139
α-helix217-2237
α-helix229-24315
α-helix249-2502
α-helix252-2554
α-helix256-2583
α-helix259-2657
α-helix271-28414
α-helix289-2979
α-helix300-3078
α-helix313-32614
α-helix331-3399
α-helix342-3498
α-helix355-36814
α-helix373-3819
α-helix385-39410
α-helix397-41115
α-helix412-4154
α-helix418-4269
α-helix430-4356
α-helix436-4383
α-helix442-46524
α-helix472-4798
α-helix482-4898
α-helix495-50814
Chain B: 35 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix89-968
α-helix101-11515
α-helix123-1286
α-helix132-1376
α-helix145-15814
α-helix163-1719
α-helix174-18411
α-helix187-20115
α-helix205-2139
α-helix217-2226
α-helix223-2253
α-helix229-24315
α-helix249-2502
α-helix252-2554
α-helix256-2583
α-helix259-2657
α-helix271-28515
α-helix289-2979
α-helix300-3078
α-helix313-32614
α-helix331-3399
α-helix342-3498
α-helix355-36915
α-helix373-3819
α-helix385-39410
α-helix397-41115
α-helix412-4154
α-helix419-4268
α-helix430-4356
α-helix436-4383
α-helix442-46524
α-helix472-4798
α-helix482-4887
α-helix489-4913
α-helix495-50814

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Karyopherin alphaA, Bprotein423Saccharomyces cerevisiaeQ02821 (AlphaFold model)
Myc proto-oncogene proteinC, D, E, Fprotein9Homo sapiensP01106 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1EE4_1 KARYOPHERIN ALPHA (chains A, B)
QELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEM
LQLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTD
YRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLI
YSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNI
VTGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIP
PLVKLLEVAEDKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIE
VTLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIE
TYF
Sequence of entity 2 (C, D, E, F), FASTA
>1EE4_2 MYC PROTO-ONCOGENE PROTEIN (chains C, D, E, F)
PAAKRVKLD

Primary citation

Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha. Conti, E., Kuriyan, J. Structure (2000) 8:329-338. DOI 10.1016/S0969-2126(00)00107-6 · PubMed

Other PDB entries of the same protein (UniProt Q02821 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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