8F19: Kap114

Cryo-EM structure of Kap114 bound to Gsp1 (RanGTP). Determined by electron microscopy at 3.49 Å resolution. Released 26 Jul 2023.

Method
Electron microscopy
Resolution
3.49 Å
Organism
Saccharomyces cerevisiae S288C
Chains
2
Atoms
8,717
Mol. weight
134.98 kDa
Ligands
MG, GTP
Released
26 Jul 2023

Explore 8F19 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8F19 contains 64 α-helices and 13 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: 58 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix3-97
α-helix15-3117
α-helix33-4513
α-helix51-6818
β-strand7111
β-strand7311
α-helix76-772
α-helix84-9714
α-helix105-12218
α-helix128-1369
α-helix137-1415
α-helix144-15613
α-helix1601
α-helix161-1655
α-helix168-18114
α-helix187-20620
α-helix213-23523
α-helix243-26321
α-helix266-2683
α-helix271-29121
α-helix302-32120
α-helix325-3273
α-helix328-34215
α-helix344-3452
α-helix346-3549
α-helix356-3649
α-helix372-38211
α-helix385-40117
α-helix406-42015
α-helix425-4262
α-helix431-44717
α-helix453-46917
α-helix477-49317
α-helix498-51215
α-helix517-5204
α-helix523-54119
α-helix548-56013
α-helix571-58616
α-helix592-60514
α-helix611-63121
α-helix633-6353
α-helix641-65515
α-helix663-6642
α-helix665-68117
α-helix685-70117
α-helix704-7074
α-helix708-7103
α-helix711-72212
α-helix728-7314
α-helix734-74411
α-helix749-76618
α-helix770-78617
α-helix788-79710
β-strand799-80022
β-strand803-80422
α-helix805-81915
α-helix823-83715
α-helix842-8454
β-strand848-84923
β-strand877-87823
α-helix879-89517
α-helix965-97713
α-helix983-9908
α-helix993-100210
Chain B: 6 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand12-1874
α-helix25-3410
β-strand47-56104
β-strand59-68104
α-helix78-814
β-strand87-9374
α-helix97-11317
β-strand119-12464
α-helix134-1363
α-helix137-1448
β-strand147-15044
α-helix161-17111
β-strand17814

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Importin subunit beta-5Aprotein1004Saccharomyces cerevisiae S288CP53067 (AlphaFold model)
GTP-binding nuclear protein GSP1/CNR1Bprotein179Saccharomyces cerevisiae S288CP32835 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8F19_1 Importin subunit beta-5 (chains A)
MDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQFALLS
LRKLITMYWSPGFESYRSTSNVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCIVQISA
VDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSEEMFFEGGIGLATMEIVFKVL
NTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLTLNFGN
VDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANVETTES
EPLLETVHDCSIYIVEFLTSVCTLQFSVEEMNKIITSLTILCQLSSETREIWTSDFNTFV
SKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIEHSTCNYSTLESLLYLLQCIL
LNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALPDIKPL
TSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIRIINQV
SSDAEEDTNGALMEVLSQVISYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVVVQSQE
CLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYSPLLSLVLEFITVFLKKKPND
GFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIMKVLER
LLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQNLLSVL
CFLTCNDPKQTVDFLSSFQIDNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSNLFFLN
DKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLYTKIIKLFVSELSFQSKQPNP
EQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDITGLMD
VKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL
Sequence of entity 2 (B), FASTA
>8F19_2 GTP-binding nuclear protein GSP1/CNR1 (chains B)
MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGE
IKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIV
LCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFV

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31

Primary citation

Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex. Jiou, J., Shaffer, J.M., Bernades, N.E. et al. Proc Natl Acad Sci U S A (2023) 120:e2301199120-e2301199120. DOI 10.1073/pnas.2301199120 · PubMed

Other PDB entries of the same protein (UniProt P53067 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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