› 6hkq

X-ray diffraction
1.54Å resolution

Human GPX4 in complex with covalent Inhibitor ML162 (S enantiomer)

Released:
DOI: 10.2210/pdb6hkq/pdb
PDB entry 6hkq coloured by chain, front view.
PDB entry 6hkq coloured by chain, side view.
PDB entry 6hkq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162.
Moosmayer D, Hilpmann A, Hoffmann J, Schnirch L, Zimmermann K, Badock V, Furst L, Eaton JK, Viswanathan VS, Schreiber SL, Gradl S, Hillig RC
OpenAccess logo Acta Crystallogr D Struct Biol 77 237-248 (2021)
PMID: 33559612

Function and Biology Details

Reactions catalysed: 
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H(2)O
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipid hydroperoxide glutathione peroxidase GPX4 Chain: A
Molecule details ›
Chain: A
Length: 176 amino acids
Theoretical weight: 20.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36969 (Residues: 28-197; Coverage: 86%)
Gene name: GPX4
Sequence domains: Glutathione peroxidase

Ligands and Environments

4 bound ligands:
Ligand G9N 1 x G9N
Ligand SO4 1 x SO4
Ligand EDO 1 x EDO
Ligand DMS 2 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 32.734Å b: 57.249Å c: 81.311Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.184
Expression system: Escherichia coli

Quick links

Citations

15 review citations

A Promising Future of Ferroptosis in Tumor Therapy.
Wang et al. (2021)
14 more

5 mentions without citation

Selenium-More than Just a Fortuitous Sulfur Substitute in Redox Biology.
Maia et al. (2023)
4 more