5MF9: RBM5 OCRE domain

Solution structure of the RBM5 OCRE domain in complex with polyproline SmN peptide. Determined by solution NMR. Released 7 Dec 2016.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
607
Mol. weight
8.57 kDa
Released
7 Dec 2016

Explore 5MF9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5MF9 contains 2 α-helices and 6 β-strands across 2 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: 1 helix, 6 β-strands

ElementResiduesLengthSheet
α-helix151
β-strand16-1831
β-strand23-2641
β-strand31-3331
β-strand40-4231
β-strand47-5151
β-strand58-6031
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix103-1042

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RNA-binding protein 5Aprotein64Homo sapiensP52756 (AlphaFold model)
Survival motor neuron proteinBprotein11Homo sapiensQ16637 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5MF9_1 RNA-binding protein 5 (chains A)
GAMGTKYAVPDTSTYQYDESSGYYYDPTTGLYYDPNSQYYYNSLTQQYLYWDGEKETYVP
AAES
Sequence of entity 2 (B), FASTA
>5MF9_2 Survival motor neuron protein (chains B)
GMRPPPPGIRG

Primary citation

Structural basis for the recognition ofspliceosomal SmN B B proteins by theRBM5 OCRE domain in splicing regulation. Mourao, A., Bonnal, S., Komal, S. et al. Elife (2016) 5:1-25. DOI 10.7554/eLife.14707 · PubMed

Other PDB entries of the same protein (UniProt P52756 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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