› 2qpj

X-ray diffraction
2.05Å resolution

Human NEP complexed with a bifunctional NEP/DPP IV inhibitor

Released:
DOI: 10.2210/pdb2qpj/pdb
PDB entry 2qpj coloured by chain, front view.
PDB entry 2qpj coloured by chain, side view.
PDB entry 2qpj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.
Oefner C, Pierau S, Schulz H, Dale GE
Acta Crystallogr D Biol Crystallogr 63 975-81 (2007)
PMID: 17704566

Function and Biology Details

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

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: Saccharomyces cerevisiae
UniProt:
  • Canonical: P08473 (Residues: 55-750; Coverage: 93%)
Gene names: EPN, MME
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NAG 3 x NAG
Ligand ZN 1 x ZN
Ligand I20 1 x I20
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P3221
Unit cell:
a: 107.123Å b: 107.123Å c: 112.375Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.207 0.268
Expression system: Saccharomyces cerevisiae

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Citations

8 review citations

Novel Therapeutic Approaches Targeting the Renin-Angiotensin System and Associated Peptides in Hypertension and Heart Failure.
Arendse et al. (2019)
7 more

7 mentions without citation

Is It Reliable to Use Common Molecular Docking Methods for Comparing the Binding Affinities of Enantiomer Pairs for Their Protein Target?
Ramírez et al. (2016)
6 more