› 5tj2

X-ray diffraction
2.8Å resolution

Gasdermin-B C-terminal domain containing the polymorphism residues Gly299:Ser306 fused to maltose binding protein

Released:
DOI: 10.2210/pdb5tj2/pdb
PDB entry 5tj2 coloured by chain, front view.
PDB entry 5tj2 coloured by chain, side view.
PDB entry 5tj2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Human Gasdermin-B and disease: Sulfatide Binding, Caspase cleavage, and Structural impact of Asthma- and IBS-Associated Polymorphism
Chao LK, Kulakova L, Herzberg O
Proc. Natl. Acad. Sci. U.S.A. (2017)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Gasdermin-B, N-terminal Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 553 amino acids
Theoretical weight: 60.46 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TAX9 (Residues: 209-211, 216-411; Coverage: 45%)
  • Best match: Q8TAX9-1 (Residues: 220-406)
Gene names: GSDMB, GSDML, PP4052, PRO2521
Sequence domains: Gasdermin PUB domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2221
Unit cell:
a: 144.039Å b: 152.75Å c: 255.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.252
Expression system: Escherichia coli

Quick links

Citations

46 review citations

Gasdermins: Effectors of Pyroptosis.
Kovacs et al. (2017)
45 more

4 mentions without citation

Gene polymorphism linked to increased asthma and IBD risk alters gasdermin-B structure, a sulfatide and phosphoinositide binding protein.
Chao et al. (2017)
3 more