6A38: MVM NS2 NES

MVM NS2 NES in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.69 Å resolution. Released 19 Jun 2019.

Method

X-ray diffraction

Resolution

2.69 Å

Organisms

Homo sapiens, Saccharomyces cerevisiae, Minute virus of mice

Chains

4

Atoms

11,075

Mol. weight

160.94 kDa

Ligands

GTP, MG

Released

19 Jun 2019

Explore 6A38 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6A38 contains 81 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

Molecules and chains

>6A38_1 GTP-binding nuclear protein Ran (chains A)
GSSHHHHHHSSGLVPRGSHMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVA
TLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNV
PNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPF
LWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQAEHDLEVAQTTALPDEDDDL

>6A38_2 Ran-specific GTPase-activating protein 1 (chains B)
GGSDIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKK
TNKVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRF
GSKENADKFKEEFEKAQEINKKA

>6A38_3 Exportin-1 (chains C)
GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF
STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK
SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA
KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL
LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL
KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE
LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEIQLYKSEREVLVYL
THLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDL
LGLCEQKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMA
CDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEE
RSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGA
DFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYIS
KARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQ
SVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKH
NNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQ
ALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFL
SALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENA

>6A38_4 MVM NS2 NES (chains D)
GGSTVDEMTKKFGTLTIHDT

Ligands and cofactors

Water and common crystallization additives (EDO, GOL, NA) 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

Related structures

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

• 3GJ0 1.48 Å, Crystal structure of human RanGDP
• 7MO5 1.55 Å, Crystal Structure of the ZnF4 of Nucleoporin NUP153 in complex with Ran-GDP
• 7MO1 1.6 Å, Crystal Structure of the ZnF1 of Nucleoporin NUP153 in complex with Ran-GDP
• 5CIQ 1.65 Å, Ran GDP wild type tetragonal crystal form
• 7MO2 1.65 Å, Crystal Structure of the ZnF2 of Nucleoporin NUP153 in complex with Ran-GDP
• 5CIT 1.75 Å, Ran GDP wild type monoclinic crystal form
• 5CIW 1.75 Å, Ran GDP Y39A mutant monoclinic crystal form
• 5CJ2 1.75 Å, Ran GDP Y39A mutant triclinic crystal form
• 1I2M 1.76 Å, Ran-RCC1-SO4 complex
• 4HAT 1.78 Å, Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1-Ran-RanBP1
• 3GJ3 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF2 complex
• 3GJ5 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF4 complex

Browse structure collections

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