4aw6

X-ray diffraction
3.4Å resolution

Crystal structure of the human nuclear membrane zinc metalloprotease ZMPSTE24 (FACE1)

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

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-131145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CAAX prenyl protease 1 homolog Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 482 amino acids
Theoretical weight: 55.71 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O75844 (Residues: 1-475; Coverage: 100%)
Gene names: FACE1, STE24, ZMPSTE24
Sequence domains:
Structure domains: Metalloproteases ("zincins"), catalytic domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P1
Unit cell:
a: 60.987Å b: 95.451Å c: 131.095Å
α: 76.73° β: 79.64° γ: 72.61°
R-values:
R R work R free
0.247 0.246 0.264
Expression system: Spodoptera frugiperda