6bh8

X-ray diffraction
3.85Å resolution

Crystal structure of ZMPSTE24 in complex with phosphoramidon

Released:
Source organism: Homo sapiens
Primary publication:
Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.
Acta Crystallogr D Struct Biol 74 739-747 (2018)
PMID: 30082509

Function and Biology Details

Reaction catalysed:
The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-131145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CAAX prenyl protease 1 homolog Chains: A, B
Molecule details ›
Chains: A, B
Length: 483 amino acids
Theoretical weight: 55.71 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: O75844 (Residues: 1-475; Coverage: 100%)
Gene names: FACE1, STE24, ZMPSTE24
Sequence domains:
Structure domains: Metalloproteases ("zincins"), catalytic domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 93.329Å b: 84.661Å c: 132.017Å
α: 90° β: 96.26° γ: 90°
R-values:
R R work R free
0.341 0.338 0.371
Expression system: Saccharomyces cerevisiae