4omd

X-ray diffraction
2.7Å resolution

X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba

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:
Non-polymer only 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
UniProt:
  • Canonical: P09958 (Residues: 108-574; Coverage: 61%)
Gene names: FUR, FURIN, PACE, PCSK3
Sequence domains:
Structure domains:
phenylacetyl-Arg-Val-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: 665 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 141.616Å b: 152.612Å c: 168.538Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.218
Expression systems:
  • Homo sapiens
  • Not provided