Zinc in PDB 5jmy: Neprilysin Complexed with LBQ657

All present enzymatic activity of Neprilysin Complexed with LBQ657:
3.4.24.11;

The structure of Neprilysin Complexed with LBQ657, PDB code: 5jmy was solved by N.Schiering, C.Wiesmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.28 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.737, 109.139, 248.003, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 22.8

The binding sites of Zinc atom in the Neprilysin Complexed with LBQ657 (pdb code 5jmy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Neprilysin Complexed with LBQ657, PDB code: 5jmy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Neprilysin Complexed with LBQ657


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Neprilysin Complexed with LBQ657 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn806 b:24.8 occ:1.00 OE1 A:GLU646 1.9 21.2 1.0 NE2 A:HIS583 1.9 21.2 1.0 NE2 A:HIS587 1.9 24.1 1.0 O24 A:6LD807 2.1 21.4 1.0 CD A:GLU646 2.7 20.8 1.0 O25 A:6LD807 2.7 22.1 1.0 C21 A:6LD807 2.8 23.8 1.0 OE2 A:GLU646 2.9 25.2 1.0 CE1 A:HIS587 2.9 25.0 1.0 CD2 A:HIS583 2.9 21.2 1.0 CE1 A:HIS583 3.0 21.2 1.0 CD2 A:HIS587 3.0 24.6 1.0 NE2 A:HIS711 3.9 22.7 1.0 ND1 A:HIS587 4.0 26.2 1.0 CG A:HIS583 4.0 20.7 1.0 CG A:HIS587 4.1 23.8 1.0 ND1 A:HIS583 4.1 22.0 1.0 CG A:GLU646 4.1 21.4 1.0 C18 A:6LD807 4.2 24.0 1.0 O A:HOH1107 4.3 40.1 1.0 CD2 A:HIS711 4.3 22.4 1.0 CB A:ALA649 4.6 19.1 1.0 OE2 A:GLU584 4.6 26.8 1.0 CB A:GLU646 4.7 17.5 1.0 OE1 A:GLU584 4.7 19.1 1.0 CA A:GLU646 4.7 15.9 1.0 O A:HOH1184 4.7 30.4 1.0 C14 A:6LD807 4.8 21.2 1.0 C16 A:6LD807 4.9 22.5 1.0

Zinc binding site 2 out of 2 in the Neprilysin Complexed with LBQ657


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Neprilysin Complexed with LBQ657 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn806 b:31.8 occ:1.00 NE2 B:HIS587 1.9 45.1 1.0 OE1 B:GLU646 1.9 21.3 1.0 O24 B:6LD807 2.0 33.5 1.0 NE2 B:HIS583 2.0 30.2 1.0 C21 B:6LD807 2.6 35.2 1.0 O25 B:6LD807 2.6 34.5 1.0 CD B:GLU646 2.7 35.7 1.0 OE2 B:GLU646 2.9 27.0 1.0 CE1 B:HIS587 2.9 44.8 1.0 CD2 B:HIS583 2.9 30.9 1.0 CD2 B:HIS587 3.0 45.1 1.0 CE1 B:HIS583 3.0 30.3 1.0 NE2 B:HIS711 3.9 24.1 1.0 ND1 B:HIS587 4.0 45.6 1.0 C18 B:6LD807 4.0 32.8 1.0 CG B:HIS583 4.0 30.7 1.0 CG B:HIS587 4.1 43.8 1.0 ND1 B:HIS583 4.1 31.3 1.0 CG B:GLU646 4.2 26.1 1.0 O B:HOH1007 4.4 33.6 1.0 CD2 B:HIS711 4.4 24.8 1.0 OE2 B:GLU584 4.5 34.2 1.0 CB B:ALA649 4.6 28.9 1.0 OE1 B:GLU584 4.6 37.7 1.0 C14 B:6LD807 4.7 23.2 1.0 C16 B:6LD807 4.7 26.2 1.0 CB B:GLU646 4.8 28.5 1.0 CA B:GLU646 4.8 27.8 1.0 CD B:GLU584 5.0 38.2 1.0 O20 B:6LD807 5.0 23.1 1.0 C22 B:6LD807 5.0 31.2 1.0

N.Schiering, A.D'arcy, F.Villard, P.Ramage, C.Logel, F.Cumin, G.M.Ksander, C.Wiesmann, R.G.Karki, M.Mogi. Structure of Neprilysin in Complex with the Active Metabolite of Sacubitril. Sci Rep V. 6 27909 2016.
ISSN: ESSN 2045-2322
PubMed: 27302413
DOI: 10.1038/SREP27909