5h5q

X-ray diffraction
1.1Å resolution

Crystal structure of human GPX4 in complex with GXpep-1

Released:

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-153273 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phospholipid hydroperoxide glutathione peroxidase GPX4 Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36969 (Residues: 29-197; Coverage: 86%)
Gene name: GPX4
Sequence domains: Glutathione peroxidase
Structure domains: Glutaredoxin
GXpep-1 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.73 KDa
Source organism: Escherichia phage T7
Expression system: Not provided

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 32.746Å b: 72.242Å c: 39.616Å
α: 90° β: 108.41° γ: 90°
R-values:
R R work R free
0.164 0.163 0.184
Expression systems:
  • Escherichia coli
  • Not provided