3M1I: Yeast CRM1

Crystal structure of yeast CRM1 (Xpo1p) in complex with yeast RanBP1 (Yrb1p) and yeast RanGTP (Gsp1pGTP). Determined by X-ray diffraction at 2.0 Å resolution. Released 2 Jun 2010.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Saccharomyces cerevisiae
Chains
3
Atoms
11,634
Mol. weight
167.66 kDa
Ligands
MG, GTP
Released
2 Jun 2010

Explore 3M1I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3M1I contains 82 α-helices and 16 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: 12 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand12-1981
α-helix25-3410
β-strand47-57111
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
α-helix161-17111
β-strand17811
α-helix180-1823
α-helix184-1874
α-helix200-2078
α-helix210-2112
Chain B: 1 helix, 7 β-strands
ElementResiduesLengthSheet
β-strand83-97152
β-strand102-116152
β-strand122-12762
β-strand134-13962
β-strand14712
β-strand155-16392
β-strand170-17782
α-helix181-19919
Chain C: 69 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix0-56
α-helix10-112
α-helix13-2513
α-helix28-4316
α-helix47-504
α-helix51-577
α-helix61-7717
α-helix79-813
α-helix84-10320
α-helix105-1106
α-helix112-12918
α-helix137-1459
α-helix149-16315
α-helix164-1685
α-helix176-20328
α-helix207-22014
α-helix227-2304
α-helix234-2396
α-helix241-2444
α-helix246-26116
α-helix262-2643
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-strand443-44533
β-strand451-45333
α-helix459-47820
α-helix480-49516
α-helix502-51413
α-helix521-53818
α-helix545-56117
α-helix563-5686
α-helix570-58314
α-helix589-60618
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-helix783-7886
α-helix789-80113
α-helix804-8063
α-helix810-82213
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-helix978-9803
α-helix987-100216
α-helix1008-102013
α-helix1025-103915
α-helix1046-10549

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein GSP1/CNR1Aprotein219Saccharomyces cerevisiaeP32835 (AlphaFold model)
Ran-specific GTPase-activating protein 1Bprotein191Saccharomyces cerevisiaeP41920 (AlphaFold model)
Exportin-1Cprotein1049Saccharomyces cerevisiaeP30822 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3M1I_1 GTP-binding nuclear protein GSP1/CNR1 (chains A)
MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGE
IKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIV
LCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVA
SPALAPPEVQVDEQLMQQYQQEMEQATALPLPDEDDADL
Sequence of entity 2 (B), FASTA
>3M1I_2 Ran-specific GTPase-activating protein 1 (chains B)
DKKEEAAPKPPSSAVFSMFGGKKAEKPETKKDEEDTKEETKKEGDDAPESPDIHFEPVVH
LEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTNKVRILMRRDK
TLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGSKENADKFKEE
FEKAQEINKKA
Sequence of entity 3 (C), FASTA
>3M1I_3 Exportin-1 (chains C)
GAMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFS
TNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKS
DLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAK
ALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELL
STKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLK
ATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEEREL
FKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREF
VKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSI
SGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRT
VILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTAD
LQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSET
VKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPK
VRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCM
TTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFL
ELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIF
VSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYL
ANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDK
ENALMEQNRLEREKAAKIGGLLKPSELDD

Ligands and cofactors

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

Primary citation

An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1. Koyama, M., Matsuura, Y. EMBO J (2010) 29:2002-2013. DOI 10.1038/emboj.2010.89 · PubMed

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

Browse structure collections

About this viewer

MolViewer shows 3M1I directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.