Sodium in PDB 5am9: Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16:
3.4.15.1;

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16, PDB code: 5am9 was solved by G.Masuyer, K.M.Larmuth, R.G.Douglas, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	113.27 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.348, 101.800, 113.950, 85.04, 85.55, 81.88
R / Rfree (%)	19.674 / 22.907

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16 also contains other interesting chemical elements:

Zinc	(Zn)	4 atoms
Calcium	(Ca)	2 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Sodium atom in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16 (pdb code 5am9). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16, PDB code: 5am9:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1003 b:30.2 occ:1.00 OE2 A:GLU262 2.3 32.1 1.0 O A:HOH2208 2.3 31.9 1.0 O A:HOH2211 2.4 35.1 1.0 OD2 A:ASP354 2.4 36.2 1.0 O A:HOH2213 2.6 30.9 1.0 OD1 A:ASN263 2.7 30.5 1.0 CD A:GLU262 3.4 30.1 1.0 CG A:ASP354 3.4 33.5 1.0 CG A:ASN263 3.7 29.6 1.0 O A:HOH2262 4.0 38.8 1.0 ND2 A:ASN263 4.0 29.2 1.0 CB A:ASP354 4.0 29.9 1.0 CG A:GLU262 4.1 28.8 1.0 O A:HOH2210 4.2 35.6 1.0 O A:HOH3003 4.3 31.6 1.0 OD1 A:ASP354 4.3 35.3 1.0 OG A:SER260 4.3 23.3 1.0 OE1 A:GLU262 4.3 28.2 1.0 O A:HOH2054 4.4 33.6 1.0 O A:HOH2206 4.4 29.6 1.0 OD2 A:ASP255 4.5 22.7 1.0 O A:HOH2265 4.7 37.3 1.0 O A:HOH2127 4.9 23.4 1.0 O A:GLY254 5.0 22.8 1.0 CB A:ASN263 5.0 29.0 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16 within 5.0Å range: probe atom residue distance (Å) B Occ D:Na1003 b:40.3 occ:1.00 O D:HOH2202 2.0 33.5 1.0 OE2 D:GLU262 2.2 31.4 1.0 OD2 D:ASP354 2.4 33.9 1.0 O D:HOH2208 2.4 33.6 1.0 OD1 D:ASN263 2.9 24.1 1.0 CD D:GLU262 3.4 27.6 1.0 CG D:ASP354 3.4 30.5 1.0 CG D:ASN263 3.8 22.1 1.0 CB D:ASP354 4.0 27.3 1.0 O D:HOH2201 4.2 21.9 1.0 ND2 D:ASN263 4.2 21.0 1.0 CG D:GLU262 4.3 25.0 1.0 OE1 D:GLU262 4.3 28.4 1.0 O D:HOH2039 4.4 34.2 1.0 OD1 D:ASP354 4.4 34.4 1.0 OG D:SER260 4.4 21.5 1.0 OD2 D:ASP255 4.5 20.8 1.0 O D:HOH2270 4.8 33.9 1.0 O D:HOH2105 4.9 17.8 1.0 O D:GLY254 4.9 20.0 1.0 O D:HOH2203 5.0 28.6 1.0

K.M.Larmuth, G.Masuyer, R.G.Douglas, E.D.Sturrock, K.R.Acharya. The Kinetic and Structural Characterisation of Amyloid-Beta Metabolism By Human Angiotensin-1- Converting Enzyme (Ace) Febs J. V. 283 1060 2016.
ISSN: ISSN 1742-464X
PubMed: 26748546
DOI: 10.1111/FEBS.13647