› 5o2z

X-ray diffraction
1.7Å resolution

Domain swap dimer of the G167R variant of gelsolin second domain

Released:
DOI: 10.2210/pdb5o2z/pdb
PDB entry 5o2z coloured by chain, front view.
PDB entry 5o2z coloured by chain, side view.
PDB entry 5o2z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Gelsolin pathogenic Gly167Arg mutation promotes domain-swap dimerization of the protein.
Bonì F, Milani M, Barbiroli A, Diomede L, Mastrangelo E, de Rosa M
Hum Mol Genet 27 53-65 (2018)
PMID: 29069428

Function and Biology Details

Biochemical function:
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-139018 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gelsolin Chains: A, B
Molecule details ›
Chains: A, B
Length: 119 amino acids
Theoretical weight: 13.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P06396 (Residues: 178-293; Coverage: 15%)
Gene name: GSN
Sequence domains: Gelsolin repeat

Ligands and Environments

5 bound ligands:
Ligand CA 2 x CA
Ligand FLC 2 x FLC
Ligand ACT 2 x ACT
Ligand NA 2 x NA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: C2
Unit cell:
a: 106.29Å b: 44.42Å c: 58.01Å
α: 90° β: 110.13° γ: 90°
R-values:
R R work R free
0.201 0.199 0.242
Expression system: Escherichia coli BL21

Quick links

Citations

8 citation in other articles

The role of gelsolin domain 3 in familial amyloidosis (Finnish type).
Zorgati et al. (2019)
7 more

1 mention without citation

Gelsolin pathogenic Gly167Arg mutation promotes domain-swap dimerization of the protein.
Bonì et al. (2018)