4il3

X-ray diffraction
3.1Å resolution

Crystal Structure of S. mikatae Ste24p

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125997 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CAAX prenyl protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 53.34 KDa
Source organism: Saccharomyces mikatae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: M4GGS2 (Residues: 1-461; Coverage: 100%)
Sequence domains:
Structure domains: Metalloproteases ("zincins"), catalytic domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P65
Unit cell:
a: 143.53Å b: 143.53Å c: 197.024Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.271 0.27 0.293
Expression system: Saccharomyces cerevisiae