Zinc in PDB 7z70: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat

Enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat, PDB code: 7z70 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) 52.15 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.563, 85.987, 134.686, 90, 90, 90
R / Rfree (%) 17.4 / 21.3

Other elements in 7z70:

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

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat (pdb code 7z70). 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 Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat, PDB code: 7z70:

Zinc binding site 1 out of 1 in 7z70

Go back to Zinc Binding Sites List in 7z70
Zinc binding site 1 out of 1 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat


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 Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn710

b:15.9
occ:1.00
 O01 A:KS8701 2.0 12.2 1.0
OE1 A:GLU411 2.0 16.3 1.0
NE2 A:HIS387 2.2 15.9 1.0
NE2 A:HIS383 2.2 14.4 1.0
CD A:GLU411 2.9 16.7 1.0
P02 A:KS8701 3.0 16.1 1.0
O03 A:KS8701 3.1 16.3 1.0
CE1 A:HIS387 3.1 16.0 1.0
CE1 A:HIS383 3.2 16.8 1.0
OE2 A:GLU411 3.2 13.9 1.0
CD2 A:HIS387 3.2 13.2 1.0
CD2 A:HIS383 3.2 16.0 1.0
HE1 A:TYR523 3.2 14.9 1.0
HE1 A:HIS387 3.2 19.2 1.0
HE1 A:HIS383 3.3 20.1 1.0
HD2 A:HIS387 3.3 15.8 1.0
HD2 A:HIS383 3.3 19.2 1.0
HA A:GLU411 3.7 16.2 1.0
O1 A:BO3703 3.8 17.4 1.0
H141 A:KS8701 3.8 16.4 1.0
H182 A:KS8701 3.9 18.5 1.0
C14 A:KS8701 4.0 13.7 1.0
CE1 A:TYR523 4.0 12.4 1.0
OH A:TYR523 4.1 15.1 1.0
ND1 A:HIS387 4.2 17.7 1.0
ND1 A:HIS383 4.3 14.6 1.0
CG A:HIS387 4.3 14.7 1.0
CG A:GLU411 4.3 16.0 1.0
CG A:HIS383 4.3 15.2 1.0
O2 A:BO3703 4.3 17.4 1.0
HB3 A:GLU411 4.4 17.7 1.0
H051 A:KS8701 4.4 16.6 1.0
HO1 A:BO3703 4.4 20.9 1.0
B A:BO3703 4.5 19.1 1.0
CA A:GLU411 4.5 13.5 1.0
C15 A:KS8701 4.5 14.0 1.0
C04 A:KS8701 4.6 12.6 1.0
O A:HOH953 4.6 14.6 1.0
CZ A:TYR523 4.6 12.7 1.0
CB A:GLU411 4.6 14.7 1.0
OE2 A:GLU384 4.6 15.9 1.0
C18 A:KS8701 4.7 15.4 1.0
HO2 A:BO3703 4.7 20.8 1.0
HG3 A:GLU411 4.7 19.2 1.0
N17 A:KS8701 4.8 13.9 1.0
HH A:TYR523 4.9 18.1 1.0
H142 A:KS8701 4.9 16.4 1.0
HG2 A:GLU411 4.9 19.2 1.0
H041 A:KS8701 4.9 15.2 1.0
H181 A:KS8701 4.9 18.5 1.0
C05 A:KS8701 4.9 13.9 1.0
H052 A:KS8701 5.0 16.6 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: Sat Apr 8 06:34:38 2023

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