X-ray diffraction
2.6Å resolution

Crystal structure of human neprilysin E584D in complex with C-type natriuretic peptide.


Function and Biology Details

Reaction catalysed:
Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Neprilysin Chain: AAA
Molecule details ›
Chain: AAA
Length: 696 amino acids
Theoretical weight: 79.51 KDa
Source organism: Homo sapiens
Expression system: Komagataella phaffii GS115
  • Canonical: P08473 (Residues: 55-750; Coverage: 93%)
Gene names: EPN, MME
Sequence domains:
C-type natriuretic peptide fragment (CNP) Chain: DDD
Molecule details ›
Chain: DDD
Length: 4 amino acids
Theoretical weight: 302 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: DIAMOND BEAMLINE I03
Spacegroup: P3221
Unit cell:
a: 109.267Å b: 109.267Å c: 112.579Å
α: 90° β: 90° γ: 120°
R R work R free
0.246 0.244 0.287
Expression systems:
  • Komagataella phaffii GS115
  • Not provided