6UT2: Leiomodin/tropomyosin binding interface

3D structure of the leiomodin/tropomyosin binding interface. Determined by solution NMR. Released 30 Sept 2020.

Method
Solution NMR
Organism
Homo sapiens
Chains
3
Atoms
870
Mol. weight
12.49 kDa
Released
30 Sept 2020

Explore 6UT2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6UT2 contains 5 α-helices and 0 β-strands across 3 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: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-64
α-helix18-214
α-helix27-4014
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix1-2828
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-2827

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Leiomodin-2Aprotein40Homo sapiensQ6P5Q4 (AlphaFold model)
Tropomyosin alpha-1 chain chimeric peptideB, Cprotein33Homo sapiensP03069 (AlphaFold model), P09493 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6UT2_1 Leiomodin-2 (chains A)
STFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIE
Sequence of entity 2 (B, C), FASTA
>6UT2_2 Tropomyosin alpha-1 chain chimeric peptide (chains B, C)
GMDAIKKKMQMLKLDNYHLENEVARLKKLVGER

Primary citation

Leiomodin creates a leaky cap at the pointed end of actin-thin filaments. Tolkatchev, D., Smith Jr., G.E., Schultz, L.E. et al. PLoS Biol (2020) 18:e3000848-e3000848. DOI 10.1371/journal.pbio.3000848 · PubMed

Other PDB entries of the same protein (UniProt Q6P5Q4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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