PDBe 3gef

X-ray diffraction
1.5Å resolution

Crystal structure of the R482W mutant of lamin A/C

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the lamin A/C R482W mutant responsible for dominant familial partial lipodystrophy (FPLD).
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 665-70 (2009)
PMID: 19574635

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lamin-A/C Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 118 amino acids
Theoretical weight: 13.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P02545 (Residues: 436-552; Coverage: 18%)
Gene names: LMN1, LMNA
Structure domains: Lamin Tail domain

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 62.195Å b: 84.035Å c: 98.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.214 0.253
Expression system: Escherichia coli