› 5syt

X-ray diffraction
2Å resolution

Crystal Structure of ZMPSTE24

Released:
DOI: 10.2210/pdb5syt/pdb
PDB entry 5syt coloured by chain, front view.
PDB entry 5syt coloured by chain, side view.
PDB entry 5syt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human CaaX protease ZMPSTE24 expressed in yeast: Structure and inhibition by HIV protease inhibitors.
Clark KM, Jenkins JL, Fedoriw N, Dumont ME
Protein Sci 26 242-257 (2017)
PMID: 27774687

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131145 (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

8 bound ligands:
Ligand SO4 2 x SO4
Ligand PC1 1 x PC1
Ligand CXE 1 x CXE
Ligand C8E 12 x C8E
Ligand ZN 1 x ZN
Ligand GOL 2 x GOL
Ligand PEG 1 x PEG
Ligand DMS 3 x DMS
No modified residues

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

Quick links

Citations

6 review citations

Membrane properties that shape the evolution of membrane enzymes.
Sanders et al. (2018)
5 more

4 mentions without citation

Translocon Declogger Ste24 Protects against IAPP Oligomer-Induced Proteotoxicity.
Kayatekin et al. (2018)
3 more