3WYG: Xpo1p-PKI-Gsp1p-GTP complex

Crystal structure of Xpo1p-PKI-Gsp1p-GTP complex. Determined by X-ray diffraction at 2.15 Å resolution. Released 12 Nov 2014.

Method
X-ray diffraction
Resolution
2.15 Å
Organisms
Saccharomyces cerevisiae AWRI796, Saccharomyces cerevisiae S288c, Homo sapiens
Chains
3
Atoms
10,368
Mol. weight
149.64 kDa
Ligands
GTP, MG
Released
12 Nov 2014

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

Secondary structure: helices and β-sheets

3WYG contains 76 α-helices and 13 β-strands across 3 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, 9 β-strands

ElementResiduesLengthSheet
β-strand12-1981
α-helix25-3410
β-strand47-56101
β-strand59-68101
α-helix72-743
α-helix78-825
β-strand87-9371
α-helix97-1015
α-helix103-11311
β-strand119-12461
α-helix135-1373
α-helix140-1445
β-strand147-15041
β-strand15212
β-strand15712
α-helix161-17111
β-strand17811
Chain C: 67 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix13-2513
α-helix28-4316
α-helix49-579
α-helix61-7818
α-helix79-813
α-helix84-10320
α-helix105-1106
α-helix112-12918
α-helix137-14610
α-helix149-16315
α-helix164-1685
β-strand17113
β-strand17413
α-helix176-20328
α-helix207-22014
α-helix227-2304
α-helix234-2363
α-helix237-2415
α-helix242-2443
α-helix246-2483
α-helix249-25911
α-helix269-28921
α-helix297-3037
α-helix308-33124
α-helix334-3363
α-helix337-35115
α-helix356-37520
α-helix417-4204
α-helix421-43313
β-strand441-44554
β-strand451-45554
α-helix460-47819
α-helix480-49516
α-helix502-51312
α-helix521-54121
α-helix545-56016
α-helix563-5686
α-helix570-58314
α-helix591-60616
α-helix608-6114
α-helix613-6142
α-helix621-6277
α-helix629-6335
α-helix638-65316
α-helix658-66811
α-helix670-68516
α-helix687-6915
α-helix693-71321
α-helix714-7174
α-helix718-74629
α-helix748-7525
α-helix754-77623
α-helix780-7823
α-helix783-7875
α-helix788-80114
α-helix804-8063
α-helix809-82214
α-helix823-8253
α-helix827-84519
α-helix853-86917
α-helix872-8765
α-helix879-89315
α-helix898-91720
α-helix922-94423
α-helix949-9513
α-helix952-96716
α-helix987-100216
α-helix1008-102114
α-helix1025-103814
α-helix1046-10505
α-helix1051-10544
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix36-438

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Gsp1pAprotein182Saccharomyces cerevisiae AWRI796P32835 (AlphaFold model)
Exportin-1Cprotein1049Saccharomyces cerevisiae S288cP30822 (AlphaFold model)
cAMP-dependent protein kinase inhibitor alphaDprotein76Homo sapiensP61925 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3WYG_1 Gsp1p (chains A)
MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGE
IKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIV
LCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVA
SP
Sequence of entity 2 (C), FASTA
>3WYG_2 Exportin-1 (chains C)
GAMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFS
TNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKS
DLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAK
ALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELL
STKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLK
ATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEEREL
FKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREF
VKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSI
SGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRT
VILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTAD
LQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSET
VKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPK
VRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCM
TTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFL
ELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIF
VSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYL
ANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDK
ENALMEQNRLEREKAAKIGGLLKPSELDD
Sequence of entity 3 (D), FASTA
>3WYG_3 cAMP-dependent protein kinase inhibitor alpha (chains D)
MTDVETTYADFIASGRTGRRNAIHDILVSSASGNLNELALKLAGLDINKTEGEEDAQRSS
TEQSGEAQGEAAKSES

Ligands and cofactors

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

Primary citation

Structural insights into how yrb2p accelerates the assembly of the xpo1p nuclear export complex. Koyama, M., Shirai, N., Matsuura, Y. Cell Rep (2014) 9:983-995. DOI 10.1016/j.celrep.2014.09.052 · PubMed

Other PDB entries of the same protein (UniProt P32835 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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