Sodium in PDB 7z6z: Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat

Protein crystallography data

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat, PDB code: 7z6z was solved by G.E.Cozier, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.46 / 1.75
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 72.575, 77.8, 81.592, 88.92, 64.62, 74.81
R / Rfree (%) 17.2 / 20

Other elements in 7z6z:

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Zinc (Zn) 2 atoms
Calcium (Ca) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat (pdb code 7z6z). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat, PDB code: 7z6z:

Sodium binding site 1 out of 1 in 7z6z

Go back to Sodium Binding Sites List in 7z6z
Sodium binding site 1 out of 1 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na723

b:46.3
occ:1.00
O A:HOH816 2.2 40.4 1.0
O A:HOH1158 2.2 41.5 1.0
OE2 A:GLU262 2.4 47.1 1.0
HG3 A:GLU262 3.1 45.7 1.0
HD21 A:ASN263 3.1 40.9 1.0
O A:HOH1146 3.2 43.2 1.0
CD A:GLU262 3.3 50.4 1.0
HB2 A:ASP354 3.4 43.5 1.0
HG2 A:GLU262 3.5 45.7 1.0
OD2 A:ASP354 3.5 43.2 1.0
CG A:GLU262 3.5 38.1 1.0
ND2 A:ASN263 3.6 34.1 1.0
CG A:ASP354 3.7 36.9 1.0
HG A:SER260 3.7 47.1 1.0
HB3 A:ASP354 3.7 43.5 1.0
HB3 A:SER260 3.8 36.5 1.0
HD22 A:ASN263 3.8 40.9 1.0
CB A:ASP354 3.8 36.3 1.0
OG A:SER260 4.0 39.3 1.0
O A:HOH966 4.2 27.1 1.0
CG A:ASN263 4.3 34.1 1.0
HB2 A:ASP255 4.3 33.2 1.0
CB A:SER260 4.4 30.4 1.0
OD1 A:ASP354 4.4 39.7 1.0
O A:HOH831 4.4 39.0 1.0
OE1 A:GLU262 4.5 55.8 1.0
OD2 A:ASP255 4.5 29.1 1.0
OD1 A:ASN263 4.6 37.4 1.0
H A:ASN263 4.7 32.1 1.0
O A:HOH1176 4.8 38.2 1.0
H A:GLU262 4.8 31.4 1.0
HB2 A:SER260 4.9 36.5 1.0
O A:SER260 5.0 25.3 1.0
CA A:CA722 5.0 65.5 1.0

Reference:

G.E.Cozier, E.C.Newby, S.L.U.Schwager, R.E.Isaac, E.D.Sturrock, K.R.Acharya. Structural Basis For the Inhibition of Human Angiotensin-1 Converting Enzyme By Fosinoprilat. Febs J. V. 289 6659 2022.
ISSN: ISSN 1742-464X
PubMed: 35653492
DOI: 10.1111/FEBS.16543
Page generated: Fri Apr 7 17:24:27 2023

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