› 3v5b

X-ray diffraction
3Å resolution

Structure of Coil 2b of human lamin

Released:
DOI: 10.2210/pdb3v5b/pdb
PDB entry 3v5b coloured by chain, front view.
PDB entry 3v5b coloured by chain, side view.
PDB entry 3v5b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the lamin A/C R335W and E347K mutants: implications for dilated cardiolaminopathies.
Bollati M, Barbiroli A, Favalli V, Arbustini E, Charron P, Bolognesi M
Biochem Biophys Res Commun 418 217-21 (2012)
PMID: 22266370

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-135892 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lamin-A/C Chain: A
Molecule details ›
Chain: A
Length: 74 amino acids
Theoretical weight: 8.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02545 (Residues: 313-386; Coverage: 11%)
Gene names: LMN1, LMNA
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6522
Unit cell:
a: 90.02Å b: 90.02Å c: 74.722Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.286 0.28 0.326
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Cellular Mechanotransduction: From Tension to Function.
Martino et al. (2018)
6 more

1 mention without citation

Lamin A/C Mechanotransduction in Laminopathies.
Donnaloja et al. (2020)