› 3g1e

X-ray diffraction
1.83Å resolution

X-ray crystal structure of coil 1A of human vimentin

Released:
DOI: 10.2210/pdb3g1e/pdb
PDB entry 3g1e coloured by chain, front view.
PDB entry 3g1e coloured by chain, side view.
PDB entry 3g1e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation.
Meier M, Padilla GP, Herrmann H, Wedig T, Hergt M, Patel TR, Stetefeld J, Aebi U, Burkhard P
J Mol Biol 390 245-61 (2009)
PMID: 19422834

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140284 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vimentin Chains: A, B
Molecule details ›
Chains: A, B
Length: 39 amino acids
Theoretical weight: 4.48 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P08670 (Residues: 102-138; Coverage: 8%)
Gene name: VIM

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P41212
Unit cell:
a: 35.496Å b: 35.496Å c: 108.022Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.253 0.295
Expression system: Not provided

Quick links

Citations

8 review citations

Intermediate filaments: primary determinants of cell architecture and plasticity.
Herrmann et al. (2009)
7 more

7 mentions without citation

Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly.
Chernyatina et al. (2012)
6 more