3EA5: GTP-binding nuclear protein Ran

Kap95p Binding Induces the Switch Loops of RanGDP to adopt the GTP-bound Conformation: Implications for Nuclear Import Complex Assembly Dynamics. Determined by X-ray diffraction at 2.5 Å resolution. Released 21 Oct 2008.

Method
X-ray diffraction
Resolution
2.5 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae
Chains
4
Atoms
16,428
Mol. weight
239.68 kDa
Ligands
MG, GDP
Released
21 Oct 2008

Explore 3EA5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EA5 contains 134 α-helices and 13 β-strands across 4 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: 8 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand10-1781
α-helix23-3210
α-helix34-363
β-strand45-54101
β-strand57-66101
α-helix70-723
α-helix76-805
β-strand85-9171
α-helix95-995
α-helix101-11111
β-strand117-12261
α-helix138-1403
β-strand144-14851
α-helix159-16911
β-strand17611
Chain B: 61 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-helix135-1428
α-helix149-16517
α-helix180-1878
α-helix195-20814
α-helix213-2164
α-helix219-23315
α-helix238-25518
α-helix256-2583
α-helix260-2623
α-helix263-2675
α-helix268-2758
α-helix280-30627
α-helix317-33216
α-helix347-36216
α-helix363-3664
α-helix367-37711
α-helix383-39412
α-helix402-41817
α-helix419-4213
α-helix425-44218
α-helix443-4453
α-helix452-46312
α-helix467-48418
α-helix491-4955
α-helix496-50712
α-helix513-5153
α-helix516-53015
α-helix533-5353
α-helix536-55419
α-helix558-5603
α-helix563-58624
α-helix588-5903
α-helix592-5943
α-helix595-60713
α-helix615-62915
α-helix630-6334
α-helix634-64916
α-helix654-67017
α-helix671-6744
α-helix675-68915
α-helix698-71316
α-helix714-7174
α-helix718-73215
α-helix734-7363
α-helix741-76424
α-helix769-7724
α-helix773-7753
α-helix776-78813
α-helix790-7934
α-helix796-81217
α-helix819-8235
α-helix825-83612
α-helix842-85918
Chain C: 6 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand10-1672
α-helix23-3210
β-strand45-55112
β-strand57-66102
α-helix70-723
α-helix76-805
β-strand85-9172
α-helix95-995
α-helix101-11111
β-strand117-12262
β-strand144-14852
α-helix159-16911
Chain D: 59 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1513
α-helix19-3517
α-helix37-4812
α-helix55-6612
α-helix74-8714
α-helix90-10415
α-helix109-12921
α-helix135-1428
α-helix149-16315
α-helix180-1878
α-helix195-20713
α-helix213-2164
α-helix219-23214
α-helix238-25518
α-helix256-2583
α-helix260-2623
α-helix263-2675
α-helix268-2758
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-helix425-44218
α-helix443-4453
α-helix452-46312
α-helix467-48418
α-helix491-4955
α-helix496-50712
α-helix513-5153
α-helix516-52914
α-helix533-5353
α-helix536-55419
α-helix563-58624
α-helix588-5903
α-helix592-5943
α-helix595-60713
α-helix615-62915
α-helix631-6333
α-helix634-64916
α-helix654-67017
α-helix671-6744
α-helix675-68915
α-helix698-71316
α-helix714-7174
α-helix718-73215
α-helix734-7363
α-helix741-76424
α-helix769-7724
α-helix773-7753
α-helix776-78813
α-helix790-7934
α-helix796-81217
α-helix819-8235
α-helix825-83511
α-helix842-85918

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein RanA, Cprotein216Homo sapiensP62826 (AlphaFold model)
Importin subunit beta-1B, Dprotein861Saccharomyces cerevisiaeQ06142 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>3EA5_1 GTP-binding nuclear protein Ran (chains A, C)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
CLAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Sequence of entity 2 (B, D), FASTA
>3EA5_2 Importin subunit beta-1 (chains B, D)
MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRIL
AALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIA
AIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNI
LIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEV
QAAAFGCLCKIMSKYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDI
AYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQ
NCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLM
NDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINL
VEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSA
SISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMG
LFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAV
GFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPY
LNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIF
QFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLF
SQATKDTARWAREQQKRQLSL

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg4
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22

Primary citation

Kap95p binding induces the switch loops of RanGDP to adopt the GTP-bound conformation: implications for nuclear import complex assembly dynamics. Forwood, J.K., Lonhienne, T.G., Marfori, M. et al. J Mol Biol (2008) 383:772-782. DOI 10.1016/j.jmb.2008.07.090 · PubMed

Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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