7dtg

X-ray diffraction
3.6Å resolution

Crystal structure of lamin B1 Ig-like domain from human

Released:
Model geometry
Fit model/data
Source organism: Homo sapiens
Primary publication:
Beta-strand-mediated dimeric formation of the Ig-like domains of human lamin A/C and B1.
Biochem Biophys Res Commun 550 191-196 (2021)
PMID: 33706103

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149030 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lamin-B1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 149 amino acids
Theoretical weight: 16.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P20700 (Residues: 407-553; Coverage: 25%)
Gene names: LMN2, LMNB, LMNB1
Sequence domains: Lamin Tail Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2221
Unit cell:
a: 144.647Å b: 160.751Å c: 132.805Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.222 0.262
Expression system: Escherichia coli BL21(DE3)