9VM1: MVM NS2 mutant Nm42

MVM NS2 mutant Nm42 in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.45 Å resolution. Released 6 Aug 2025.

Method
X-ray diffraction
Resolution
2.45 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae S288C, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains
4
Atoms
11,191
Mol. weight
161.05 kDa
Ligands
MG, GTP
Released
6 Aug 2025

Explore 9VM1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VM1 contains 82 α-helices and 14 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: 11 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand9-1681
α-helix23-3210
β-strand45-54101
β-strand57-66101
α-helix76-805
β-strand85-9171
α-helix95-995
α-helix101-11111
β-strand117-12261
α-helix133-1353
α-helix139-1424
β-strand145-14841
α-helix159-16911
β-strand17611
α-helix178-1869
α-helix191-1933
α-helix194-20512
α-helix208-2092
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-strand170-17892
α-helix181-19515
Chain C: 69 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1-55
α-helix10-112
α-helix13-2412
α-helix28-4215
α-helix47-504
α-helix51-577
α-helix61-7818
α-helix79-813
α-helix84-10320
α-helix105-1106
α-helix112-12918
α-helix137-1459
α-helix149-16315
α-helix164-1685
α-helix170-1734
α-helix176-18813
α-helix190-20314
α-helix207-22014
α-helix227-2304
α-helix234-2396
α-helix241-2444
α-helix246-25914
α-helix269-28921
α-helix297-3037
α-helix308-32619
α-helix327-3304
α-helix337-35014
α-helix356-37520
α-helix417-4204
α-helix421-43313
α-helix462-47817
α-helix480-49516
α-helix502-51413
α-helix521-54121
α-helix545-56117
α-helix563-5686
α-helix570-58314
α-helix591-60616
α-helix608-6114
α-helix621-6277
α-helix629-6335
α-helix638-65316
α-helix658-66811
α-helix670-68516
α-helix689-6913
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-helix872-8754
α-helix879-89315
α-helix898-91619
α-helix922-94423
α-helix949-9513
α-helix952-96716
α-helix9771
α-helix987-100216
α-helix1008-102013
α-helix1025-103814
α-helix1046-10505
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix77-8711

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein RanAprotein235Homo sapiensP62826 (AlphaFold model)
Ran-specific GTPase-activating protein 1Bprotein143Saccharomyces cerevisiae S288CP41920 (AlphaFold model)
Exportin-1Cprotein1003Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P30822 (AlphaFold model)
Asp-gly-tyr-ile-glu-glu-leu-ile-arg-met-phe-gly-lys-leu-ser-ile-his-asp-aspDprotein19Homo sapiens
Sequence of entity 1 (A), FASTA
>9VM1_1 GTP-binding nuclear protein Ran (chains A)
GSSHHHHHHSSGLVPRGSHMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVA
TLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNV
PNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPF
LWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Sequence of entity 2 (B), FASTA
>9VM1_2 Ran-specific GTPase-activating protein 1 (chains B)
GGSDIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKK
TNKVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRF
GSKENADKFKEEFEKAQEINKKA
Sequence of entity 3 (C), FASTA
>9VM1_3 Exportin-1 (chains C)
GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF
STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK
SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA
KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL
LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL
KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE
LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEIQLYKSEREVLVYL
THLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDL
LGLCEQKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMA
CDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEE
RSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGA
DFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYIS
KARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQ
SVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKH
NNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQ
ALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFL
SALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENA
Sequence of entity 4 (D), FASTA
>9VM1_4 ASP-GLY-TYR-ILE-GLU-GLU-LEU-ILE-ARG-MET-PHE-GLY-LYS-LEU-SER-ILE-HIS-ASP-ASP (chains D)
DGYIEELIRMFGKLSIHDD

Ligands and cofactors

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

Water and common crystallization additives (NO3, NA, GOL) are not listed.

Primary citation

Cancer Therapy with Nanoparticle-Medicated Intracellular Expression of Peptide CRM1-Inhibitor. Sui, M., Xiong, M., Li, Y. et al. Int J Nanomedicine (2021) 16:2833-2847. DOI 10.2147/IJN.S266398 · 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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