› 2xv5

X-ray diffraction
2.4Å resolution

Human lamin A coil 2B fragment

Released:
DOI: 10.2210/pdb2xv5/pdb
PDB entry 2xv5 coloured by chain, front view.
PDB entry 2xv5 coloured by chain, side view.
PDB entry 2xv5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Simultaneous formation of right- and left-handed anti-parallel coiled-coil interfaces by a coil2 fragment of human lamin A.
Kapinos LE, Burkhard P, Herrmann H, Aebi U, Strelkov SV
J Mol Biol 408 135-46 (2011)
PMID: 21354179

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135893 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lamin-A/C Chains: A, B
Molecule details ›
Chains: A, B
Length: 74 amino acids
Theoretical weight: 8.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02545 (Residues: 328-398; 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
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 35.093Å b: 50.114Å c: 89.745Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.241 0.284
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Broken nuclei--lamins, nuclear mechanics, and disease.
Davidson et al. (2014)
3 more

8 mentions without citation

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