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Zinc in PDB 6h5x: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

Enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

All present enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6h5x 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) 44.60 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.160, 76.953, 83.088, 88.83, 64.22, 75.21
R / Rfree (%) 16.4 / 20.4

Other elements in 6h5x:

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

Magnesium (Mg) 1 atom
Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. (pdb code 6h5x). 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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6h5x:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6h5x

Go back to Zinc Binding Sites List in 6h5x
Zinc binding site 1 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.


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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn708

b:25.6
occ:1.00
OE1 A:GLU389 2.0 27.2 1.0
NE2 A:HIS365 2.1 24.8 1.0
NE2 A:HIS361 2.1 24.4 1.0
S2 A:FT8709 2.4 33.3 1.0
O4 A:FT8709 2.6 31.3 1.0
CE1 A:HIS361 3.0 24.5 1.0
CD A:GLU389 3.0 27.1 1.0
CE1 A:HIS365 3.0 25.0 1.0
C11 A:FT8709 3.1 31.1 1.0
CD2 A:HIS365 3.1 23.9 1.0
CD2 A:HIS361 3.1 23.8 1.0
HE1 A:HIS361 3.2 29.4 1.0
HE1 A:HIS365 3.2 30.0 1.0
HD2 A:HIS365 3.3 28.7 1.0
HD2 A:HIS361 3.3 28.6 1.0
OE2 A:GLU389 3.3 26.6 1.0
C12 A:FT8709 3.4 33.3 1.0
HE1 A:TYR501 3.6 30.0 1.0
HH A:TYR501 3.7 32.3 1.0
HA A:GLU389 3.8 32.1 1.0
N2 A:FT8709 4.0 28.4 1.0
ND1 A:HIS361 4.1 24.9 1.0
ND1 A:HIS365 4.1 25.3 1.0
C13 A:FT8709 4.2 34.7 1.0
CG A:HIS361 4.2 23.2 1.0
CG A:HIS365 4.2 24.0 1.0
OE2 A:GLU362 4.3 30.4 1.0
H22 A:EDO717 4.4 76.5 1.0
CG A:GLU389 4.4 26.9 1.0
HB3 A:GLU389 4.5 32.0 1.0
C3 A:FT8709 4.5 26.9 1.0
OH A:TYR501 4.5 26.9 1.0
CE1 A:TYR501 4.5 25.0 1.0
OE1 A:GLU362 4.6 31.0 1.0
O A:HOH973 4.6 31.5 1.0
CA A:GLU389 4.6 26.7 1.0
CD A:GLU362 4.7 30.1 1.0
CB A:GLU389 4.7 26.7 1.0
HG3 A:GLU389 4.8 32.3 1.0
HA A:GLU362 4.8 29.5 1.0
HO2 A:EDO717 4.8 77.3 1.0
HD1 A:HIS361 4.9 29.8 1.0
HD1 A:HIS365 4.9 30.4 1.0
HG2 A:GLU389 5.0 32.3 1.0
CZ A:TYR501 5.0 26.2 1.0

Zinc binding site 2 out of 2 in 6h5x

Go back to Zinc Binding Sites List in 6h5x
Zinc binding site 2 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.


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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn710

b:25.1
occ:1.00
OE1 B:GLU389 2.0 23.4 1.0
NE2 B:HIS365 2.0 24.2 1.0
NE2 B:HIS361 2.1 22.1 1.0
S2 B:FT8711 2.4 30.4 1.0
O4 B:FT8711 2.6 30.6 1.0
CD B:GLU389 3.0 23.6 1.0
CE1 B:HIS361 3.0 22.8 1.0
CE1 B:HIS365 3.0 24.6 1.0
CD2 B:HIS365 3.0 25.1 1.0
C11 B:FT8711 3.1 31.1 1.0
CD2 B:HIS361 3.1 22.3 1.0
HE1 B:HIS361 3.2 27.3 1.0
HE1 B:HIS365 3.2 29.5 1.0
HD2 B:HIS365 3.2 30.1 1.0
OE2 B:GLU389 3.3 23.2 1.0
HD2 B:HIS361 3.3 26.8 1.0
C12 B:FT8711 3.4 32.2 1.0
HE1 B:TYR501 3.6 27.9 1.0
HH B:TYR501 3.7 28.9 1.0
HA B:GLU389 3.8 27.7 1.0
N2 B:FT8711 4.0 28.4 1.0
ND1 B:HIS361 4.1 22.6 1.0
ND1 B:HIS365 4.1 25.3 1.0
C13 B:FT8711 4.2 34.6 1.0
CG B:HIS361 4.2 22.6 1.0
CG B:HIS365 4.2 25.0 1.0
OE2 B:GLU362 4.3 30.4 1.0
CG B:GLU389 4.3 23.1 1.0
HB3 B:GLU389 4.4 28.2 1.0
O2 B:EDO718 4.5 65.6 1.0
OH B:TYR501 4.5 24.1 1.0
CE1 B:TYR501 4.5 23.3 1.0
C3 B:FT8711 4.5 27.7 1.0
OE1 B:GLU362 4.5 29.2 1.0
O B:HOH979 4.6 26.7 1.0
CA B:GLU389 4.6 23.1 1.0
CB B:GLU389 4.7 23.5 1.0
CD B:GLU362 4.7 28.8 1.0
HO2 B:EDO718 4.7 78.7 1.0
HG3 B:GLU389 4.8 27.7 1.0
HA B:GLU362 4.9 27.4 1.0
HD1 B:HIS361 4.9 27.1 1.0
HD1 B:HIS365 4.9 30.4 1.0
HG2 B:GLU389 4.9 27.7 1.0
CZ B:TYR501 5.0 23.2 1.0

Reference:

G.E.Cozier, L.B.Arendse, S.L.Schwager, E.D.Sturrock, K.R.Acharya. Molecular Basis For Multiple Omapatrilat Binding Sites Within the Ace C-Domain: Implications For Drug Design. J. Med. Chem. V. 61 10141 2018.
ISSN: ISSN 1520-4804
PubMed: 30372620
DOI: 10.1021/ACS.JMEDCHEM.8B01309
Page generated: Wed Dec 16 11:55:41 2020

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