X-ray diffraction
2.15Å resolution

X-ray structure of human furin in complex with the competitive inhibitor para-guanidinomethyl-Phac-R-Tle-R-Amba


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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Furin Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 482 amino acids
Theoretical weight: 52.39 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
  • Canonical: P09958 (Residues: 108-574; Coverage: 61%)
Gene names: FUR, FURIN, PACE, PCSK3
Sequence domains:
Structure domains:
para-guanidinomethyl-phenylacetyl-Arg-(3-methylvaline)-Arg-(amidomethyl)benzamidine Chains: H, I, J, K, L, N
Molecule details ›
Chains: H, I, J, K, L, N
Length: 5 amino acids
Theoretical weight: 750 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 141.652Å b: 152.701Å c: 168.398Å
α: 90° β: 90° γ: 90°
R R work R free
0.186 0.186 0.219
Expression systems:
  • Homo sapiens
  • Not provided