5wqt

X-ray diffraction
2.64Å resolution

Structure of a protein involved in pyroptosis

Released:
Source organism: Homo sapiens
Primary publication:
Structure insight of GSDMD reveals the basis of GSDMD autoinhibition in cell pyroptosis.
Proc Natl Acad Sci U S A 114 10642-10647 (2017)
PMID: 28928145

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-157626 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gasdermin-D, C-terminal Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 22.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P57764 (Residues: 276-484; Coverage: 43%)
Gene names: DFNA5L, FKSG10, GSDMD, GSDMDC1
Sequence domains: Gasdermin PUB domain

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 47.886Å b: 86.165Å c: 112.145Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.235 0.286
Expression system: Escherichia coli BL21(DE3)