Zinc in PDB 6xvp: Crystal Structure of Neprilysin in Complex with Sampatrilat.

All present enzymatic activity of Crystal Structure of Neprilysin in Complex with Sampatrilat.:
3.4.24.11;

The structure of Crystal Structure of Neprilysin in Complex with Sampatrilat., PDB code: 6xvp was solved by G.E.Cozier, K.R.Acharya, U.Sharma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.04 / 2.65
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.089, 108.089, 112.826, 90.00, 90.00, 120.00
R / Rfree (%)	19.1 / 23.7

The binding sites of Zinc atom in the Crystal Structure of Neprilysin in Complex with Sampatrilat. (pdb code 6xvp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Neprilysin in Complex with Sampatrilat., PDB code: 6xvp:

Zinc binding site 1 out of 1 in the Crystal Structure of Neprilysin in Complex with Sampatrilat.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Neprilysin in Complex with Sampatrilat. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn801 b:33.4 occ:1.00 OE1 A:GLU646 2.0 43.2 1.0 NE2 A:HIS587 2.0 46.4 1.0 NE2 A:HIS583 2.0 40.2 1.0 O39 A:D0Z802 2.2 45.1 1.0 CD A:GLU646 2.6 38.3 1.0 OE2 A:GLU646 2.6 36.4 1.0 O40 A:D0Z802 2.7 45.6 1.0 C38 A:D0Z802 2.8 45.2 1.0 CE1 A:HIS587 2.8 47.6 1.0 CE1 A:HIS583 2.9 43.8 1.0 HE1 A:HIS587 2.9 57.2 1.0 HE1 A:HIS583 3.1 52.5 1.0 CD2 A:HIS587 3.1 47.5 1.0 CD2 A:HIS583 3.1 43.7 1.0 HD2 A:HIS587 3.3 57.0 1.0 HD2 A:HIS583 3.4 52.4 1.0 HE2 A:HIS711 3.5 56.4 1.0 C22 A:D0Z802 3.9 33.6 1.0 ND1 A:HIS587 4.0 48.8 1.0 HA A:GLU646 4.0 51.2 1.0 HD2 A:HIS711 4.0 55.9 1.0 ND1 A:HIS583 4.1 45.2 1.0 CG A:GLU646 4.1 41.6 1.0 CG A:HIS587 4.1 50.3 1.0 NE2 A:HIS711 4.1 47.0 1.0 HB3 A:ALA649 4.2 48.4 1.0 CG A:HIS583 4.2 47.3 1.0 C16 A:D0Z802 4.2 44.7 1.0 CD2 A:HIS711 4.4 46.6 1.0 HB3 A:GLU646 4.4 52.9 1.0 HB1 A:ALA649 4.5 48.4 1.0 HG3 A:GLU646 4.5 50.0 1.0 HG2 A:GLU646 4.6 50.0 1.0 HH22 A:ARG717 4.6 47.1 1.0 CB A:ALA649 4.7 40.4 1.0 OE1 A:GLU584 4.7 40.3 1.0 CB A:GLU646 4.7 44.0 1.0 HD1 A:HIS587 4.7 58.5 1.0 HB2 A:ALA649 4.7 48.4 1.0 O13 A:D0Z802 4.7 64.5 1.0 CA A:GLU646 4.8 42.6 1.0 C18 A:D0Z802 4.8 36.7 1.0 HD1 A:HIS583 4.8 54.2 1.0 C17 A:D0Z802 4.9 40.4 1.0

U.Sharma, G.E.Cozier, E.D.Sturrock, K.R.Acharya. Molecular Basis For Omapatrilat and Sampatrilat Binding to Neprilysin - Implications For Dual Inhibitor Design with Angiotensin Converting Enzyme. J.Med.Chem. 2020.
ISSN: ISSN 0022-2623
PubMed: 32337993
DOI: 10.1021/ACS.JMEDCHEM.0C00441