› 5zz0

X-ray diffraction
2.64Å resolution

HUMAN GELSOLIN FROM RESIDUES GLU28 TO ARG161 WITH CALCIUM

Released:
DOI: 10.2210/pdb5zz0/pdb
PDB entry 5zz0 coloured by chain, front view.
PDB entry 5zz0 coloured by chain, side view.
PDB entry 5zz0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Bonsai Gelsolin Survives Heat Induced Denaturation by Forming β-Amyloids which Leach Out Functional Monomer.
Badmalia MD, Sharma P, Yadav SPS, Singh S, Khatri N, Garg R
Sci Rep 8 12602 (2018)
PMID: 30135452

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139010 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gelsolin Chains: A, G
Molecule details ›
Chains: A, G
Length: 134 amino acids
Theoretical weight: 15.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P06396 (Residues: 55-188; Coverage: 18%)
Gene name: GSN
Sequence domains: Gelsolin repeat

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand PG0 1 x PG0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 35.393Å b: 63.566Å c: 98.136Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.254
Expression system: Escherichia coli BL21

Quick links

Citations

2 citation in other articles

Heat induces end to end repetitive association in P. furiosus L-asparaginase which enables its thermophilic property.
Sharma et al. (2020)
1 more

1 mention without citation

Bonsai Gelsolin Survives Heat Induced Denaturation by Forming β-Amyloids which Leach Out Functional Monomer.
Badmalia et al. (2018)