Zinc in PDB 5lv0: Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product

All present enzymatic activity of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product:
3.4.24.16;

The structure of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product, PDB code: 5lv0 was solved by G.Masuyer, R.P.-A.Berntsson, P.F.Teixeira, B.Kmiec, E.Glaser, P.Stenmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	109.11 / 2.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	131.341, 131.341, 195.979, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 26

The structure of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product (pdb code 5lv0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product, PDB code: 5lv0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:46.4 occ:1.00 OE1 A:GLU503 2.1 43.8 1.0 NE2 A:HIS478 2.3 45.4 1.0 NE2 A:HIS474 2.4 48.3 1.0 OXT C:VAL6 2.7 72.7 1.0 O C:VAL6 2.7 73.7 1.0 CD A:GLU503 2.9 44.0 1.0 OE2 A:GLU503 2.9 43.2 1.0 CD2 A:HIS474 3.0 48.4 1.0 C C:VAL6 3.0 71.8 1.0 CD2 A:HIS478 3.1 45.8 1.0 CE1 A:HIS478 3.4 46.0 1.0 CE1 A:HIS474 3.6 48.7 1.0 OG A:SER506 3.7 48.0 1.0 O C:VAL5 3.9 66.9 1.0 CB A:SER506 4.0 48.2 1.0 CG A:HIS474 4.2 49.0 1.0 NE2 A:GLN475 4.3 48.9 1.0 CA C:VAL6 4.3 70.5 1.0 CG A:GLU503 4.3 44.4 1.0 CE1 A:TYR613 4.3 47.0 1.0 CG A:HIS478 4.4 46.5 1.0 C C:VAL5 4.4 68.1 1.0 N C:VAL6 4.4 70.0 1.0 ND1 A:HIS478 4.5 46.5 1.0 ND1 A:HIS474 4.5 49.1 1.0 OE1 A:GLN475 4.6 47.6 1.0 OH A:TYR613 4.6 47.4 1.0 CD A:GLN475 4.8 48.2 1.0 CZ A:TYR613 4.9 47.1 1.0 OH A:TYR606 5.0 45.0 1.0 CB A:GLU503 5.0 44.6 1.0 CG1 C:VAL5 5.0 68.3 1.0

Zinc binding site 2 out of 2 in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:46.7 occ:1.00 OE1 B:GLU503 2.2 45.8 1.0 NE2 B:HIS474 2.3 50.7 1.0 NE2 B:HIS478 2.4 47.0 1.0 O D:VAL6 2.5 74.9 1.0 OE2 B:GLU503 2.7 46.4 1.0 CD B:GLU503 2.8 46.3 1.0 OXT D:VAL6 2.8 73.4 1.0 C D:VAL6 3.0 72.7 1.0 CD2 B:HIS474 3.1 50.7 1.0 CE1 B:HIS478 3.3 47.3 1.0 CD2 B:HIS478 3.4 47.5 1.0 CE1 B:HIS474 3.4 51.0 1.0 OG B:SER506 3.7 51.3 1.0 CB B:SER506 4.1 51.8 1.0 CE2 B:TYR613 4.2 44.6 1.0 CG B:GLU503 4.3 46.6 1.0 NE2 B:GLN475 4.3 55.3 1.0 CG B:HIS474 4.3 51.5 1.0 CA D:VAL6 4.4 71.7 1.0 OH B:TYR613 4.4 44.4 1.0 ND1 B:HIS478 4.4 48.0 1.0 O D:VAL5 4.4 68.8 1.0 ND1 B:HIS474 4.5 51.4 1.0 CG B:HIS478 4.5 48.2 1.0 N D:VAL6 4.6 71.4 1.0 CZ B:TYR613 4.7 44.7 1.0 C D:VAL5 4.7 69.3 1.0 OH B:TYR606 4.8 42.9 1.0 CB B:GLU503 5.0 47.3 1.0 CG1 D:VAL5 5.0 69.2 1.0 OE1 B:GLN475 5.0 55.3 1.0

P.F.Teixeira, G.Masuyer, C.Pinho, R.M.M.Branca, B.Kmiec, C.Wallin, S.Warmlander, R.P.-A.Berntsson, M.Ankarcrona, A.Graslund, J.Lehtio, P.Stenmark, E.Glaser. Structural and Functional Analysis of Neurolysin, A New Component of the Mitochondrial Peptidolytic Network To Be Published.