2X19: Importin13 - RanGTP complex

Crystal structure of Importin13 - RanGTP complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 16 Feb 2010.

Method
X-ray diffraction
Resolution
2.8 Å
Organisms
SACCHAROMYCES CEREVISIAE, HOMO SAPIENS
Chains
2
Atoms
8,440
Mol. weight
129.69 kDa
Ligands
GTP, MG
Released
16 Feb 2010

Explore 2X19 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2X19 contains 71 α-helices and 10 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: 9 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand12-1981
α-helix25-3410
α-helix36-383
β-strand47-5591
β-strand5612
β-strand60-6891
α-helix72-743
α-helix78-814
β-strand87-9371
α-helix97-1015
α-helix103-11311
β-strand119-12461
α-helix135-1373
α-helix140-1423
β-strand146-15051
β-strand15213
β-strand15713
α-helix161-17010
β-strand17812
Chain B: 62 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix23-3513
α-helix39-5416
α-helix58-658
α-helix72-8817
α-helix90-923
α-helix95-973
α-helix98-11114
α-helix117-13418
α-helix142-1509
α-helix160-17718
α-helix195-1973
α-helix198-20912
α-helix216-23015
α-helix236-2383
α-helix240-24910
α-helix256-26712
α-helix272-2743
α-helix276-28712
α-helix290-2989
α-helix302-32524
α-helix327-3293
α-helix330-34415
α-helix355-3606
α-helix361-37111
α-helix376-40126
α-helix406-4105
α-helix414-43825
α-helix440-45112
α-helix452-4565
α-helix463-47614
α-helix487-4948
α-helix495-4973
α-helix503-51513
α-helix517-5226
α-helix524-5274
α-helix531-5377
α-helix541-5433
α-helix544-55714
α-helix559-5613
α-helix566-57813
α-helix584-59815
α-helix603-62523
α-helix631-65020
α-helix676-69520
α-helix699-71517
α-helix721-7233
α-helix724-73714
α-helix741-75414
α-helix762-78120
α-helix787-80317
α-helix805-8095
α-helix815-82511
α-helix831-84414
α-helix845-8473
α-helix853-8575
α-helix862-87110
α-helix872-8765
α-helix879-8813
α-helix882-89514
α-helix897-90711
α-helix920-93011
α-helix937-95216

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein GSP1/CNR1Aprotein172SACCHAROMYCES CEREVISIAEP32835 (AlphaFold model)
Importin-13Bprotein963HOMO SAPIENSO94829 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2X19_1 GTP-BINDING NUCLEAR PROTEIN GSP1/CNR1 (chains A)
GEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGEIKFDVWD
TAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVD
VKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFV
Sequence of entity 2 (B), FASTA
>2X19_2 IMPORTIN-13 (chains B)
MERREEQPGAAGAGAAPALDFTVENVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWH
FSWQLLQPDKVPEIQYFGASALHIKISRYWSDIPTDQYESLKAQLFTQITRFASGSKIVL
TRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTS
RLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCE
ALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRYVNTLLKLIPLVLGLQEQLRQAVQNG
DMETSHGICRIAVALGENHSRALLDQVEHWQSFLALVNMIMFCTGIPGHYPVNETTSSLT
LTFWYTLQDDILSFEAEKQAVYQQVYRPVYFQLVDVLLHKAQFPSDEEYGFWSSDEKEQF
RIYRVDISDTLMYVYEMLGAELLSNLYDKLGRLLTSSEEPYSWQHTEALLYGFQSIAETI
DVNYSDVVPGLIGLIPRISISNVQLADTVMFTIGALSEWLADHPVMINSVLPLVLHALGN
PELSVSSVSTLKKICRECKYDLPPYAANIVAVSQDVLMKQIHKTSQCMWLMQALGFLLSA
LQVEEILKNLHSLISPYIQQLEKLAEEIPNPSNKLAIVHILGLLSNLFTTLDISHHEDDH
EGPELRKLPVPQGPNPVVVVLQQVFQLIQKVLSKWLNDAQVVEAVCAIFEKSVKTLLDDF
APMVPQLCEMLGRMYSTIPQASALDLTRQLVHIFAHEPAHFPPIEALFLLVTSVTLTLFQ
QGPRDHPDIVDSFMQLLAQALKRKPDLFLCERLDVKAVFQCAVLALKFPEAPTVKASCGF
FTELLPRCGEVESVGKVVQEDGRMLLIAVLEAIGGQASRSLMDCFADILFALNKHCFSLL
SMWIKEALQPPGFPSARLSPEQKDTFSQQILRERVNKRRVKEMVKEFTLLCRGLHGTDYT
ADY

Ligands and cofactors

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

Primary citation

Nuclear Import Mechanism of the Ejc Component Mago- Y14 Revealed by Structural Studies of Importin 13. Bono, F., Cook, A.G., Grunwald, M. et al. Mol Cell (2010) 37:211. DOI 10.1016/J.MOLCEL.2010.01.007 · 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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