5syt

X-ray diffraction
2Å resolution

Crystal Structure of ZMPSTE24

Released:

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CAAX prenyl protease 1 homolog Chain: A
Molecule details ›
Chain: A
Length: 480 amino acids
Theoretical weight: 55.33 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: O75844 (Residues: 1-474; Coverage: 100%)
Gene names: FACE1, STE24, ZMPSTE24
Sequence domains:

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 149.455Å b: 84.56Å c: 76.885Å
α: 90° β: 119.07° γ: 90°
R-values:
R R work R free
0.219 0.218 0.249
Expression system: Saccharomyces cerevisiae