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:
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
|