› 6bwk

X-ray diffraction
2.79Å resolution

Crystal structure of the human MLKL pseudokinase domain T357E/S358E mutant

Released:
DOI: 10.2210/pdb6bwk/pdb
PDB entry 6bwk coloured by chain, front view.
PDB entry 6bwk coloured by chain, side view.
PDB entry 6bwk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis.
Petrie EJ, Sandow JJ, Jacobsen AV, Smith BJ, Griffin MDW, Lucet IS, Dai W, Young SN, Tanzer MC, Wardak A, Liang LY, Cowan AD, Hildebrand JM, Kersten WJA, Lessene G, Silke J, Czabotar PE, Webb AI, Murphy JM
Nat Commun 9 2422 (2018)
PMID: 29930286

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-185458 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mixed lineage kinase domain-like protein Chain: A
Molecule details ›
Chain: A
Length: 287 amino acids
Theoretical weight: 32.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NB16 (Residues: 190-471; Coverage: 60%)
Gene name: MLKL
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2221
Unit cell:
a: 72.114Å b: 74.723Å c: 127.601Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.255 0.297
Expression system: Escherichia coli

Quick links

Citations

31 review citations

Pore formation in regulated cell death.
Flores-Romero et al. (2020)
30 more

2 mentions without citation

Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis.
Petrie et al. (2018)
1 more