Zinc 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
Sodium (Na) 1 atom
Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat, PDB code: 7z6z:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7z6z

Go back to Zinc Binding Sites List in 7z6z
Zinc binding site 1 out of 2 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 Zinc with other atoms in the Zn 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:Zn718

b:19.6
occ:1.00
OE1 A:GLU389 2.0 20.3 1.0
O01 A:KS8701 2.0 19.5 1.0
NE2 A:HIS365 2.1 20.7 1.0
NE2 A:HIS361 2.2 22.7 1.0
CD A:GLU389 2.9 21.3 1.0
CE1 A:HIS365 3.0 23.7 1.0
P02 A:KS8701 3.0 19.6 1.0
O03 A:KS8701 3.1 21.4 1.0
HE1 A:HIS365 3.1 28.4 1.0
CD2 A:HIS361 3.1 21.0 1.0
CE1 A:HIS361 3.1 22.7 1.0
OE2 A:GLU389 3.1 20.7 1.0
CD2 A:HIS365 3.2 19.8 1.0
HE1 A:TYR501 3.2 22.9 1.0
HD2 A:HIS361 3.3 25.1 1.0
HE1 A:HIS361 3.3 27.2 1.0
HD2 A:HIS365 3.4 23.7 1.0
HA A:GLU389 3.6 25.2 1.0
H141 A:KS8701 3.9 24.7 1.0
CE1 A:TYR501 4.0 19.1 1.0
H182 A:KS8701 4.0 23.2 1.0
C14 A:KS8701 4.1 20.6 1.0
OH A:TYR501 4.1 20.1 1.0
HO1 A:PEG702 4.1 42.3 1.0
ND1 A:HIS365 4.1 22.3 1.0
ND1 A:HIS361 4.2 20.2 1.0
CG A:HIS361 4.2 20.3 1.0
CG A:HIS365 4.2 20.9 1.0
CG A:GLU389 4.3 19.8 1.0
H051 A:KS8701 4.4 24.4 1.0
O A:HOH907 4.4 19.5 1.0
HB3 A:GLU389 4.5 25.7 1.0
CZ A:TYR501 4.5 19.3 1.0
CA A:GLU389 4.5 21.0 1.0
O A:HOH969 4.5 19.1 1.0
C04 A:KS8701 4.5 19.8 1.0
C15 A:KS8701 4.6 20.9 1.0
O1 A:PEG702 4.6 35.2 1.0
OE2 A:GLU362 4.7 20.3 1.0
CB A:GLU389 4.7 21.4 1.0
HG3 A:GLU389 4.7 23.7 1.0
HH A:TYR501 4.8 24.1 1.0
C18 A:KS8701 4.8 19.4 1.0
H041 A:KS8701 4.8 23.7 1.0
N17 A:KS8701 4.8 21.7 1.0
HG2 A:GLU389 4.8 23.7 1.0
C05 A:KS8701 4.9 20.4 1.0
HD1 A:HIS365 4.9 26.7 1.0
H142 A:KS8701 4.9 24.7 1.0
HD1 A:HIS361 5.0 24.2 1.0
H052 A:KS8701 5.0 24.4 1.0

Zinc binding site 2 out of 2 in 7z6z

Go back to Zinc Binding Sites List in 7z6z
Zinc binding site 2 out of 2 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 Zinc with other atoms in the Zn binding site number 2 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
B:Zn713

b:24.6
occ:1.00
OE1 B:GLU389 1.8 22.2 1.0
O01 B:KS8701 2.1 23.8 1.0
NE2 B:HIS365 2.1 26.9 1.0
NE2 B:HIS361 2.2 22.6 1.0
CD B:GLU389 2.8 26.7 1.0
HE1 B:HIS365 2.8 34.8 1.0
CE1 B:HIS365 2.8 29.0 1.0
O03 B:KS8701 3.0 26.7 1.0
P02 B:KS8701 3.0 22.7 1.0
CD2 B:HIS361 3.0 24.2 1.0
OE2 B:GLU389 3.1 26.0 1.0
HD2 B:HIS361 3.1 29.0 1.0
CE1 B:HIS361 3.2 25.8 1.0
HE1 B:TYR501 3.2 27.0 1.0
CD2 B:HIS365 3.3 28.5 1.0
HE1 B:HIS361 3.4 31.0 1.0
HA B:GLU389 3.6 32.0 1.0
HD2 B:HIS365 3.7 34.1 1.0
H141 B:KS8701 3.8 30.0 1.0
C14 B:KS8701 4.0 25.0 1.0
H182 B:KS8701 4.0 28.6 1.0
CE1 B:TYR501 4.0 22.5 1.0
ND1 B:HIS365 4.0 27.1 1.0
OH B:TYR501 4.1 23.6 1.0
CG B:GLU389 4.2 25.3 1.0
CG B:HIS361 4.2 24.4 1.0
ND1 B:HIS361 4.2 25.2 1.0
HO1 B:PEG704 4.3 55.3 1.0
CG B:HIS365 4.3 28.3 1.0
HB3 B:GLU389 4.3 33.9 1.0
H051 B:KS8701 4.4 29.9 1.0
O B:HOH941 4.5 25.1 1.0
C15 B:KS8701 4.5 23.4 1.0
CA B:GLU389 4.5 26.7 1.0
O B:HOH929 4.5 24.1 1.0
CZ B:TYR501 4.5 21.8 1.0
CB B:GLU389 4.6 28.3 1.0
C04 B:KS8701 4.6 23.8 1.0
HG3 B:GLU389 4.6 30.3 1.0
OE2 B:GLU362 4.7 26.6 1.0
HG2 B:GLU389 4.7 30.3 1.0
HD1 B:HIS365 4.8 32.5 1.0
C18 B:KS8701 4.8 23.8 1.0
N17 B:KS8701 4.8 23.1 1.0
HH B:TYR501 4.8 28.3 1.0
H142 B:KS8701 4.8 30.0 1.0
C05 B:KS8701 4.9 24.9 1.0
H041 B:KS8701 5.0 28.5 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: Sat Apr 8 06:34:38 2023

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