3TRT: Stabilised vimentin coil2 fragment

Crystal structure of stabilised vimentin coil2 fragment. Determined by X-ray diffraction at 2.3 Å resolution. Released 1 Feb 2012.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
2
Atoms
1,260
Mol. weight
18.32 kDa
Released
1 Feb 2012

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

Secondary structure: helices and β-sheets

3TRT contains 3 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-helix266-33469
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix266-30338
α-helix306-33328

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
VimentinA, Bprotein77Homo sapiensP08670 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3TRT_1 Vimentin (chains A, B)
GGSKPDCTAAMRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTE
YRRQVQSLTMEVDALKG

Primary citation

Stabilization of vimentin coil2 fragment via an engineered disulfide. Chernyatina, A.A., Strelkov, S.V. J Struct Biol (2012) 177:46-53. DOI 10.1016/j.jsb.2011.11.014 · PubMed

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

Browse structure collections

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