Zinc in PDB 6zpq: Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.
Enzymatic activity of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.
All present enzymatic activity of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.:
3.4.15.1;
Protein crystallography data
The structure of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpq
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)
|
80.50 /
1.85
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
74.683,
99.934,
128.701,
97.76,
90.21,
111.06
|
R / Rfree (%)
|
18.4 /
21.4
|
Other elements in 6zpq:
The structure of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.
(pdb code 6zpq). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpq:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 6zpq
Go back to
Zinc Binding Sites List in 6zpq
Zinc binding site 1 out
of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.
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 the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn719
b:28.7
occ:1.00
|
NE2
|
A:HIS361
|
2.0
|
24.5
|
1.0
|
OE1
|
A:GLU389
|
2.0
|
32.6
|
1.0
|
O
|
A:HOH817
|
2.0
|
23.8
|
1.0
|
NE2
|
A:HIS365
|
2.1
|
24.9
|
1.0
|
CD
|
A:GLU389
|
2.8
|
30.6
|
1.0
|
CD2
|
A:HIS361
|
2.9
|
27.3
|
1.0
|
CE1
|
A:HIS365
|
3.0
|
24.0
|
1.0
|
CE1
|
A:HIS361
|
3.0
|
29.5
|
1.0
|
OE2
|
A:GLU389
|
3.0
|
28.7
|
1.0
|
HD2
|
A:HIS361
|
3.1
|
32.8
|
1.0
|
CD2
|
A:HIS365
|
3.1
|
27.4
|
1.0
|
HE1
|
A:HIS365
|
3.1
|
28.7
|
1.0
|
HE1
|
A:HIS361
|
3.2
|
35.4
|
1.0
|
HD2
|
A:HIS365
|
3.3
|
32.9
|
1.0
|
O
|
A:HOH1058
|
3.6
|
36.8
|
1.0
|
OE2
|
A:GLU362
|
3.7
|
30.0
|
1.0
|
HA
|
A:GLU389
|
3.7
|
30.5
|
1.0
|
O
|
A:HOH993
|
4.1
|
38.1
|
1.0
|
CG
|
A:HIS361
|
4.1
|
26.4
|
1.0
|
ND1
|
A:HIS361
|
4.1
|
25.1
|
1.0
|
ND1
|
A:HIS365
|
4.1
|
24.2
|
1.0
|
CG
|
A:HIS365
|
4.2
|
24.2
|
1.0
|
CG
|
A:GLU389
|
4.2
|
29.8
|
1.0
|
O
|
A:HOH910
|
4.3
|
39.1
|
1.0
|
CD
|
A:GLU362
|
4.3
|
29.6
|
1.0
|
HG2
|
A:GLU389
|
4.3
|
35.7
|
1.0
|
O
|
A:HOH1010
|
4.4
|
25.5
|
1.0
|
HA3
|
A:GLY392
|
4.5
|
31.6
|
1.0
|
OE1
|
A:GLU362
|
4.5
|
29.3
|
1.0
|
CA
|
A:GLU389
|
4.6
|
25.4
|
1.0
|
HA
|
A:GLU362
|
4.7
|
27.6
|
1.0
|
HG3
|
A:GLU389
|
4.8
|
35.7
|
1.0
|
HD1
|
A:HIS361
|
4.9
|
30.1
|
1.0
|
HD1
|
A:HIS365
|
4.9
|
29.0
|
1.0
|
CB
|
A:GLU389
|
4.9
|
23.2
|
1.0
|
HO4
|
A:BCN707
|
5.0
|
51.6
|
1.0
|
|
Zinc binding site 2 out
of 4 in 6zpq
Go back to
Zinc Binding Sites List in 6zpq
Zinc binding site 2 out
of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.
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 the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn715
b:27.8
occ:1.00
|
O
|
B:HOH860
|
1.9
|
25.0
|
1.0
|
NE2
|
B:HIS365
|
1.9
|
25.3
|
1.0
|
OE1
|
B:GLU389
|
2.1
|
23.7
|
1.0
|
NE2
|
B:HIS361
|
2.1
|
30.2
|
1.0
|
CE1
|
B:HIS365
|
2.9
|
31.3
|
1.0
|
CD
|
B:GLU389
|
2.9
|
29.5
|
1.0
|
CD2
|
B:HIS361
|
2.9
|
28.3
|
1.0
|
HD2
|
B:HIS361
|
3.0
|
33.9
|
1.0
|
CD2
|
B:HIS365
|
3.0
|
30.2
|
1.0
|
HE1
|
B:HIS365
|
3.0
|
37.5
|
1.0
|
OE2
|
B:GLU389
|
3.1
|
23.6
|
1.0
|
CE1
|
B:HIS361
|
3.2
|
31.4
|
1.0
|
HD2
|
B:HIS365
|
3.3
|
36.2
|
1.0
|
HE1
|
B:HIS361
|
3.5
|
37.7
|
1.0
|
O
|
B:HOH820
|
3.7
|
36.5
|
1.0
|
OE2
|
B:GLU362
|
3.7
|
29.6
|
1.0
|
O
|
B:HOH1027
|
3.7
|
36.6
|
1.0
|
HA
|
B:GLU389
|
3.8
|
29.6
|
1.0
|
ND1
|
B:HIS365
|
4.0
|
26.8
|
1.0
|
O
|
B:HOH1123
|
4.0
|
51.8
|
1.0
|
CG
|
B:HIS365
|
4.1
|
28.1
|
1.0
|
CG
|
B:HIS361
|
4.2
|
25.4
|
1.0
|
ND1
|
B:HIS361
|
4.3
|
27.4
|
1.0
|
CG
|
B:GLU389
|
4.3
|
25.0
|
1.0
|
CD
|
B:GLU362
|
4.3
|
33.1
|
1.0
|
OE1
|
B:GLU362
|
4.3
|
31.0
|
1.0
|
O
|
B:HOH910
|
4.4
|
26.1
|
1.0
|
O
|
B:HOH834
|
4.4
|
34.4
|
1.0
|
HG2
|
B:GLU389
|
4.5
|
30.0
|
1.0
|
H42
|
B:BCN706
|
4.6
|
44.3
|
1.0
|
HA3
|
B:GLY392
|
4.6
|
24.8
|
1.0
|
CA
|
B:GLU389
|
4.7
|
24.6
|
1.0
|
HA
|
B:GLU362
|
4.7
|
29.6
|
1.0
|
HD1
|
B:HIS365
|
4.8
|
32.1
|
1.0
|
HG3
|
B:GLU389
|
4.9
|
30.0
|
1.0
|
CB
|
B:GLU389
|
5.0
|
23.4
|
1.0
|
|
Zinc binding site 3 out
of 4 in 6zpq
Go back to
Zinc Binding Sites List in 6zpq
Zinc binding site 3 out
of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn712
b:27.0
occ:1.00
|
O
|
C:HOH815
|
2.0
|
24.0
|
1.0
|
NE2
|
C:HIS365
|
2.0
|
26.3
|
1.0
|
OE1
|
C:GLU389
|
2.0
|
24.8
|
1.0
|
NE2
|
C:HIS361
|
2.0
|
26.0
|
1.0
|
CD
|
C:GLU389
|
2.9
|
28.4
|
1.0
|
CE1
|
C:HIS365
|
2.9
|
27.9
|
1.0
|
CD2
|
C:HIS361
|
2.9
|
23.8
|
1.0
|
HE1
|
C:HIS365
|
3.0
|
33.5
|
1.0
|
HD2
|
C:HIS361
|
3.1
|
28.6
|
1.0
|
CE1
|
C:HIS361
|
3.1
|
30.3
|
1.0
|
OE2
|
C:GLU389
|
3.1
|
25.3
|
1.0
|
CD2
|
C:HIS365
|
3.1
|
27.6
|
1.0
|
HE1
|
C:HIS361
|
3.3
|
36.3
|
1.0
|
HD2
|
C:HIS365
|
3.4
|
33.1
|
1.0
|
OE2
|
C:GLU362
|
3.6
|
28.0
|
1.0
|
HA
|
C:GLU389
|
3.7
|
28.8
|
1.0
|
O
|
C:HOH1056
|
3.8
|
34.8
|
1.0
|
O
|
C:HOH888
|
3.8
|
41.4
|
1.0
|
O
|
C:HOH1086
|
4.0
|
49.3
|
1.0
|
ND1
|
C:HIS365
|
4.1
|
24.4
|
1.0
|
CG
|
C:HIS361
|
4.1
|
24.7
|
1.0
|
ND1
|
C:HIS361
|
4.2
|
25.7
|
1.0
|
CG
|
C:HIS365
|
4.2
|
26.6
|
1.0
|
CD
|
C:GLU362
|
4.3
|
29.4
|
1.0
|
CG
|
C:GLU389
|
4.3
|
25.9
|
1.0
|
OE1
|
C:GLU362
|
4.4
|
25.9
|
1.0
|
O
|
C:HOH836
|
4.4
|
34.2
|
1.0
|
HG2
|
C:GLU389
|
4.4
|
31.1
|
1.0
|
O
|
C:HOH861
|
4.4
|
25.7
|
1.0
|
HA3
|
C:GLY392
|
4.6
|
29.7
|
1.0
|
CA
|
C:GLU389
|
4.6
|
24.0
|
1.0
|
HA
|
C:GLU362
|
4.7
|
28.5
|
1.0
|
HD1
|
C:HIS365
|
4.8
|
29.2
|
1.0
|
H42
|
C:BCN706
|
4.9
|
43.7
|
1.0
|
HG3
|
C:GLU389
|
4.9
|
31.1
|
1.0
|
HD1
|
C:HIS361
|
5.0
|
30.8
|
1.0
|
|
Zinc binding site 4 out
of 4 in 6zpq
Go back to
Zinc Binding Sites List in 6zpq
Zinc binding site 4 out
of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn715
b:28.0
occ:1.00
|
O
|
D:HOH869
|
1.8
|
24.1
|
1.0
|
OE1
|
D:GLU389
|
2.0
|
27.5
|
1.0
|
NE2
|
D:HIS361
|
2.1
|
29.1
|
1.0
|
NE2
|
D:HIS365
|
2.1
|
26.6
|
1.0
|
CD
|
D:GLU389
|
2.8
|
24.6
|
1.0
|
CD2
|
D:HIS361
|
2.9
|
27.8
|
1.0
|
HD2
|
D:HIS361
|
3.0
|
33.4
|
1.0
|
OE2
|
D:GLU389
|
3.0
|
26.3
|
1.0
|
CD2
|
D:HIS365
|
3.0
|
31.1
|
1.0
|
CE1
|
D:HIS365
|
3.1
|
26.9
|
1.0
|
HD2
|
D:HIS365
|
3.2
|
37.3
|
1.0
|
CE1
|
D:HIS361
|
3.2
|
28.9
|
1.0
|
HE1
|
D:HIS365
|
3.3
|
32.3
|
1.0
|
HE1
|
D:HIS361
|
3.5
|
34.7
|
1.0
|
O
|
D:HOH1069
|
3.7
|
31.9
|
1.0
|
OE2
|
D:GLU362
|
3.7
|
30.9
|
1.0
|
O
|
D:HOH815
|
3.7
|
39.2
|
1.0
|
HA
|
D:GLU389
|
3.7
|
25.4
|
1.0
|
CG
|
D:HIS361
|
4.1
|
26.1
|
1.0
|
O
|
D:HOH990
|
4.1
|
53.1
|
1.0
|
ND1
|
D:HIS365
|
4.2
|
29.0
|
1.0
|
CG
|
D:HIS365
|
4.2
|
30.4
|
1.0
|
HO1
|
D:EDO712
|
4.2
|
58.7
|
0.6
|
CG
|
D:GLU389
|
4.2
|
28.2
|
1.0
|
ND1
|
D:HIS361
|
4.2
|
27.6
|
1.0
|
CD
|
D:GLU362
|
4.3
|
40.8
|
1.0
|
HG2
|
D:GLU389
|
4.4
|
33.9
|
1.0
|
OE1
|
D:GLU362
|
4.4
|
31.6
|
1.0
|
O
|
D:HOH964
|
4.4
|
31.5
|
1.0
|
O
|
D:HOH825
|
4.4
|
38.5
|
1.0
|
HA3
|
D:GLY392
|
4.5
|
31.9
|
1.0
|
H11
|
D:EDO712
|
4.6
|
52.5
|
0.6
|
CA
|
D:GLU389
|
4.6
|
21.2
|
1.0
|
HA
|
D:GLU362
|
4.7
|
30.9
|
1.0
|
HG3
|
D:GLU389
|
4.8
|
33.9
|
1.0
|
HO4
|
D:BCN707
|
4.9
|
50.3
|
1.0
|
O1
|
D:EDO712
|
4.9
|
48.9
|
0.6
|
CB
|
D:GLU389
|
5.0
|
23.6
|
1.0
|
HD1
|
D:HIS365
|
5.0
|
34.7
|
1.0
|
|
Reference:
G.E.Cozier,
L.Lubbe,
E.D.Sturrock,
K.R.Acharya.
Angiotensin-Converting Enzyme Open For Business: Structural Insights Into the Sub-Domain Dynamics. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 33067882
DOI: 10.1111/FEBS.15601
Page generated: Tue Oct 29 15:52:51 2024
|