6gid

X-ray diffraction
1.9Å resolution

High resolution crystal structure of substrate-free human neprilysin

Released:
Source organism: Homo sapiens
Primary publication:
High resolution crystal structure of substrate-free human neprilysin.
J Struct Biol 204 19-25 (2018)
PMID: 29906506

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140129 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neprilysin Chain: A
Molecule details ›
Chain: A
Length: 696 amino acids
Theoretical weight: 79.53 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P08473 (Residues: 55-750; Coverage: 93%)
Gene names: EPN, MME
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P3221
Unit cell:
a: 107.424Å b: 107.424Å c: 112.316Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.235
Expression system: Komagataella pastoris