› 5tib

X-ray diffraction
2.6Å resolution

Gasdermin-B C-terminal domain containing the polymorphism residues Arg299:Ser306 fused to maltose binding protein

Released:
DOI: 10.2210/pdb5tib/pdb
PDB entry 5tib coloured by chain, front view.
PDB entry 5tib coloured by chain, side view.
PDB entry 5tib 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
Molecule details ›
Chains: A, B
Length: 557 amino acids
Theoretical weight: 61.09 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TAX9 (Residues: 209-211, 216-411; Coverage: 46%)
  • 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
2 bound ligands:
Ligand ACT 1 x ACT
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P43212
Unit cell:
a: 104.06Å b: 104.06Å c: 252.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.233
Expression system: Escherichia coli

Quick links

Citations

46 review citations

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

5 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)
4 more