5M9E: Microtubule integrity protein mal3

Interactions between the Mal3 EB1-like domain and Dis1. Determined by X-ray diffraction at 2.83 Å resolution. Released 7 Dec 2016.

Method
X-ray diffraction
Resolution
2.83 Å
Organisms
Schizosaccharomyces pombe 972h-, Schizosaccharomyces pombe
Chains
8
Atoms
2,805
Mol. weight
45.32 kDa
Released
7 Dec 2016

Explore 5M9E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5M9E contains 12 α-helices and 4 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.

Chains A, B and D: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix175-22046
α-helix227-23812
Chain C: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix175-21743
α-helix218-2225
α-helix227-23812
Chains E and F: 1 helix, 2 β-strands
ElementResiduesLengthSheet
β-strand83511
α-helix842-8454
β-strand84812
Chain G: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix842-8443

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Microtubule integrity protein mal3A, B, C, Dprotein77Schizosaccharomyces pombe 972h-Q10113 (AlphaFold model)
Phosphoprotein p93E, F, G, Hprotein20Schizosaccharomyces pombeQ09933 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5M9E_1 Microtubule integrity protein mal3 (chains A, B, C, D)
SGSAKQAQQQITSLETQLYEVNETMFGLERERDFYFNKLREIEILVQTHLTTSPMSMENM
LERIQAILYSTEDGFEL
Sequence of entity 2 (E, F, G, H), FASTA
>5M9E_2 Phosphoprotein p93 (chains E, F, G, H)
RRSLAGSMLQKPTQFSRPSF

Primary citation

An unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation. Matsuo, Y., Maurer, S.P., Yukawa, M. et al. J Cell Sci (2016) 129:4592-4606. DOI 10.1242/jcs.197533 · PubMed

Other PDB entries of the same protein (UniProt Q10113 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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