3BAS: PDB entry 3BAS

Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form. Determined by X-ray diffraction at 2.3 Å resolution. Released 8 Jan 2008.

Method
X-ray diffraction
Resolution
2.3 Å
Organisms
Argopecten irradians, Saccharomyces cerevisiae
Chains
2
Atoms
1,445
Mol. weight
21.25 kDa
Released
8 Jan 2008

Explore 3BAS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BAS contains 2 α-helices and 0 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, 0 β-strands

ElementResiduesLengthSheet
α-helix841-91676
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix838-91679

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin heavy chain, striated muscle/General control protein GCN4 chimeraA, Bprotein89Argopecten irradians, Saccharomyces cerevisiaeP03069 (AlphaFold model), P24733 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3BAS_1 Myosin heavy chain, striated muscle/General control protein GCN4 chimera (chains A, B)
GSHMPLLSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFGSMKQ
LEDKVEELLSKNYHLENEVARLKKLVGER

Primary citation

An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins. Brown, J.H., Yang, Y., Reshetnikova, L. et al. J Mol Biol (2008) 375:1434-1443. DOI 10.1016/j.jmb.2007.11.071 · PubMed

Other PDB entries of the same protein (UniProt P03069 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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