4MBE: Sac3:Sus1:Cdc31:Nup1 complex

Sac3:Sus1:Cdc31:Nup1 complex. Determined by X-ray diffraction at 2.61 Å resolution. Released 2 Jul 2014.

Method
X-ray diffraction
Resolution
2.61 Å
Organism
Saccharomyces cerevisiae
Chains
10
Atoms
5,085
Mol. weight
84.72 kDa
Ligands
CA
Released
2 Jul 2014

Explore 4MBE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MBE contains 28 α-helices and 10 β-strands across 7 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, 4 β-strands

ElementResiduesLengthSheet
α-helix19-3214
β-strand39-4021
α-helix42-509
α-helix58-6811
β-strand76-7721
α-helix78-9013
α-helix94-10512
β-strand112-11322
α-helix115-12410
α-helix131-1399
β-strand149-15022
α-helix151-1599
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix757-80448
Chain C: 5 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix5-1814
α-helix21-3515
α-helix38-5013
α-helix62-7110
α-helix75-9016
β-strand9313
Chain D: 8 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix19-3214
β-strand39-4024
α-helix42-509
α-helix58-6811
β-strand76-7724
α-helix78-9013
α-helix94-10512
β-strand112-11325
α-helix115-12410
α-helix131-1399
β-strand149-15025
α-helix151-1588
Chain E: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix756-80449
Chain F: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix9-1810
α-helix21-3515
α-helix38-5013
α-helix58-7114
α-helix75-8915
Chain X: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand32913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cell division control protein 31A, Dprotein161Saccharomyces cerevisiaeP06704 (AlphaFold model)
Nuclear mRNA export protein SAC3B, Eprotein53Saccharomyces cerevisiaeP46674 (AlphaFold model)
Protein SUS1C, Fprotein96Saccharomyces cerevisiaeQ6WNK7 (AlphaFold model)
Nucleoporin NUP1G, H, X, Yprotein25Saccharomyces cerevisiaeP20676 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>4MBE_1 Cell division control protein 31 (chains A, D)
MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKRE
ILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRR
VAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS
Sequence of entity 2 (B, E), FASTA
>4MBE_2 Nuclear mRNA export protein SAC3 (chains B, E)
EANYRKDFIDTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEKWQAS
Sequence of entity 3 (C, F), FASTA
>4MBE_3 Protein SUS1 (chains C, F)
MTMDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKSEMNINESTNFTQ
ILSTVEPKALEMVSDSTRETVLKQIREFLEEIVDTQ
Sequence of entity 4 (G, H, X, Y), FASTA
>4MBE_4 Nucleoporin NUP1 (chains G, H, X, Y)
LKKNIEPKKDKESIVLPTVGFDFIK

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export. Jani, D., Valkov, E., Stewart, M. Nucleic Acids Res (2014) 42:6686-6697. DOI 10.1093/nar/gku252 · PubMed

Other PDB entries of the same protein (UniProt P06704 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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