3G1E: Coil 1A of human vimentin

X-ray crystal structure of coil 1A of human vimentin. Determined by X-ray diffraction at 1.83 Å resolution. Released 5 May 2009.

Method
X-ray diffraction
Resolution
1.83 Å
Chains
2
Atoms
687
Mol. weight
8.97 kDa
Released
5 May 2009

Explore 3G1E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G1E 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-helix104-13734
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix106-13732

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
VimentinA, Bprotein39P08670 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3G1E_1 Vimentin (chains A, B)
XNEKVELQELNDRFANLIDKVRFLEQQNKILLAELEQLX

Primary citation

Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation. Meier, M., Padilla, G.P., Herrmann, H. et al. J Mol Biol (2009) 390:245-261. DOI 10.1016/j.jmb.2009.04.067 · PubMed

Other PDB entries of the same protein (UniProt P08670 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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