PDBe 5jxg

X-ray diffraction
1.8Å resolution

Structure of the unliganded form of the proprotein convertase furin.

Released:

Function and Biology Details

Reaction catalysed:
Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Furin Chain: A
Molecule details ›
Chain: A
Length: 482 amino acids
Theoretical weight: 52.39 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P09958 (Residues: 108-574; Coverage: 61%)
Gene names: FUR, FURIN, PACE, PCSK3
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6522
Unit cell:
a: 131.957Å b: 131.957Å c: 155.634Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.154 0.173
Expression system: Homo sapiens