3ND2: Yeast Importin-beta

Structure of Yeast Importin-beta (Kap95p). Determined by X-ray diffraction at 2.4 Å resolution. Released 7 Jul 2010.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
6,759
Mol. weight
94.84 kDa
Released
7 Jul 2010

Explore 3ND2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3ND2 contains 60 α-helices and 0 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: 60 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-1513
α-helix19-3517
α-helix37-4812
α-helix55-6612
α-helix74-8714
α-helix90-10415
α-helix109-12618
α-helix127-1293
α-helix134-1429
α-helix149-16517
α-helix172-1754
α-helix177-18812
α-helix195-20814
α-helix213-2164
α-helix219-23315
α-helix238-25518
α-helix256-2583
α-helix260-2623
α-helix263-2675
α-helix268-2736
α-helix274-2763
α-helix280-30627
α-helix317-33216
α-helix347-36216
α-helix363-3664
α-helix367-37711
α-helix383-39513
α-helix402-41817
α-helix419-4213
α-helix425-44117
α-helix443-4453
α-helix452-46211
α-helix467-48418
α-helix492-4954
α-helix496-50712
α-helix513-5153
α-helix516-53015
α-helix533-5353
α-helix536-55318
α-helix558-5603
α-helix563-58624
α-helix591-60717
α-helix611-62919
α-helix630-6367
α-helix637-64812
α-helix655-67016
α-helix675-69016
α-helix698-71316
α-helix714-7207
α-helix721-73212
α-helix734-7363
α-helix741-76525
α-helix769-7724
α-helix773-7753
α-helix776-78813
α-helix790-7934
α-helix796-81217
α-helix819-8213
α-helix825-83612
α-helix842-86019

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Importin subunit beta-1Aprotein861Saccharomyces cerevisiaeQ06142 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3ND2_1 Importin subunit beta-1 (chains A)
MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRIL
AALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIA
AIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNI
LIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEV
QAAAFGCLCKIMSLYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDI
AYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQ
NCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLM
NDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINL
VEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSA
SISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMG
LFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAV
GFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPY
LNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIF
QFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLF
SQATKDTARWAREQQKRQLSL

Primary citation

Quantitative Structural Analysis of Importin-beta Flexibility: Paradigm for Solenoid Protein Structures. Forwood, J.K., Lange, A., Zachariae, U. et al. Structure (2010) 18:1171-1183. DOI 10.1016/j.str.2010.06.015 · PubMed

Other PDB entries of the same protein (UniProt Q06142 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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