Chlorine 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:
Chlorine Binding Sites:
The binding sites of Chlorine 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 Chlorine atom.
In total 4 binding sites of Chlorine where determined in the
Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpq:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 6zpq
Go back to
Chlorine Binding Sites List in 6zpq
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl720
b:26.4
occ:1.00
|
HH
|
A:TYR202
|
2.2
|
31.4
|
1.0
|
|
HE
|
A:ARG500
|
2.3
|
37.3
|
1.0
|
|
HB3
|
A:ARG500
|
2.8
|
33.4
|
1.0
|
|
HH21
|
A:ARG500
|
2.9
|
36.9
|
1.0
|
|
HB2
|
A:PRO497
|
3.0
|
35.6
|
1.0
|
|
OH
|
A:TYR202
|
3.0
|
26.2
|
1.0
|
|
H
|
A:ARG500
|
3.0
|
31.2
|
1.0
|
|
HB2
|
A:PRO385
|
3.0
|
38.1
|
1.0
|
|
HE1
|
A:TYR202
|
3.1
|
33.4
|
1.0
|
|
NE
|
A:ARG500
|
3.1
|
31.1
|
1.0
|
|
O
|
A:HOH1091
|
3.1
|
26.9
|
1.0
|
|
HG22
|
A:ILE499
|
3.2
|
30.6
|
1.0
|
|
HE3
|
A:TRP201
|
3.2
|
33.9
|
1.0
|
|
HZ3
|
A:TRP201
|
3.3
|
35.7
|
1.0
|
|
HG2
|
A:PRO385
|
3.4
|
34.3
|
1.0
|
|
HG23
|
A:ILE499
|
3.5
|
30.6
|
1.0
|
|
HB3
|
A:PRO497
|
3.6
|
35.6
|
1.0
|
|
NH2
|
A:ARG500
|
3.6
|
30.7
|
1.0
|
|
CB
|
A:ARG500
|
3.6
|
27.8
|
1.0
|
|
CB
|
A:PRO497
|
3.7
|
29.7
|
1.0
|
|
N
|
A:ARG500
|
3.7
|
26.0
|
1.0
|
|
HG2
|
A:ARG500
|
3.7
|
32.1
|
1.0
|
|
CB
|
A:PRO385
|
3.7
|
31.8
|
1.0
|
|
CE1
|
A:TYR202
|
3.7
|
27.8
|
1.0
|
|
CG2
|
A:ILE499
|
3.8
|
25.6
|
1.0
|
|
HB3
|
A:PRO385
|
3.8
|
38.1
|
1.0
|
|
CZ
|
A:ARG500
|
3.8
|
29.2
|
1.0
|
|
CE3
|
A:TRP201
|
3.9
|
28.3
|
1.0
|
|
CZ
|
A:TYR202
|
3.9
|
27.5
|
1.0
|
|
CZ3
|
A:TRP201
|
3.9
|
29.8
|
1.0
|
|
CG
|
A:ARG500
|
4.0
|
26.8
|
1.0
|
|
CG
|
A:PRO385
|
4.1
|
28.6
|
1.0
|
|
CA
|
A:ARG500
|
4.1
|
24.6
|
1.0
|
|
HA
|
A:ARG500
|
4.1
|
29.5
|
1.0
|
|
CD
|
A:ARG500
|
4.1
|
27.5
|
1.0
|
|
HG21
|
A:ILE499
|
4.2
|
30.6
|
1.0
|
|
HG2
|
A:PRO497
|
4.3
|
40.8
|
1.0
|
|
H
|
A:ILE499
|
4.3
|
30.6
|
1.0
|
|
HB2
|
A:ARG500
|
4.4
|
33.4
|
1.0
|
|
HH22
|
A:ARG500
|
4.4
|
36.9
|
1.0
|
|
CG
|
A:PRO497
|
4.6
|
34.0
|
1.0
|
|
N
|
A:ILE499
|
4.7
|
25.5
|
1.0
|
|
C
|
A:ILE499
|
4.7
|
23.3
|
1.0
|
|
HD2
|
A:ARG500
|
4.7
|
33.0
|
1.0
|
|
HD2
|
A:PRO385
|
4.7
|
29.6
|
1.0
|
|
HG3
|
A:PRO385
|
4.7
|
34.3
|
1.0
|
|
HD3
|
A:ARG500
|
4.8
|
33.0
|
1.0
|
|
C
|
A:PRO497
|
4.8
|
26.8
|
1.0
|
|
H
|
A:TYR498
|
4.8
|
28.7
|
1.0
|
|
CA
|
A:PRO497
|
4.9
|
23.7
|
1.0
|
|
N
|
A:TYR498
|
4.9
|
23.9
|
1.0
|
|
HB3
|
A:TRP198
|
4.9
|
32.7
|
1.0
|
|
HG3
|
A:ARG500
|
5.0
|
32.1
|
1.0
|
|
O
|
A:HOH971
|
5.0
|
27.0
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 6zpq
Go back to
Chlorine Binding Sites List in 6zpq
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl716
b:23.7
occ:1.00
|
HH
|
B:TYR202
|
2.3
|
28.6
|
1.0
|
|
HE
|
B:ARG500
|
2.3
|
29.5
|
1.0
|
|
HB3
|
B:ARG500
|
2.7
|
27.3
|
1.0
|
|
HH21
|
B:ARG500
|
2.8
|
33.9
|
1.0
|
|
HB2
|
B:PRO497
|
3.0
|
29.7
|
1.0
|
|
HG22
|
B:ILE499
|
3.0
|
23.7
|
1.0
|
|
H
|
B:ARG500
|
3.0
|
27.7
|
1.0
|
|
HB2
|
B:PRO385
|
3.0
|
29.5
|
1.0
|
|
OH
|
B:TYR202
|
3.1
|
23.8
|
1.0
|
|
O
|
B:HOH1014
|
3.1
|
28.3
|
1.0
|
|
NE
|
B:ARG500
|
3.2
|
24.6
|
1.0
|
|
HE2
|
B:TYR202
|
3.2
|
25.4
|
1.0
|
|
HE3
|
B:TRP201
|
3.3
|
36.4
|
1.0
|
|
HG2
|
B:PRO385
|
3.4
|
29.2
|
1.0
|
|
HZ3
|
B:TRP201
|
3.4
|
35.9
|
1.0
|
|
NH2
|
B:ARG500
|
3.5
|
28.3
|
1.0
|
|
HB3
|
B:PRO497
|
3.6
|
29.7
|
1.0
|
|
CB
|
B:ARG500
|
3.6
|
22.7
|
1.0
|
|
N
|
B:ARG500
|
3.7
|
23.1
|
1.0
|
|
HG23
|
B:ILE499
|
3.7
|
23.7
|
1.0
|
|
CB
|
B:PRO385
|
3.7
|
24.6
|
1.0
|
|
CB
|
B:PRO497
|
3.7
|
24.7
|
1.0
|
|
CG2
|
B:ILE499
|
3.7
|
19.8
|
1.0
|
|
HG2
|
B:ARG500
|
3.8
|
28.5
|
1.0
|
|
HB3
|
B:PRO385
|
3.8
|
29.5
|
1.0
|
|
CZ
|
B:ARG500
|
3.8
|
32.0
|
1.0
|
|
CE2
|
B:TYR202
|
3.8
|
21.1
|
1.0
|
|
CZ
|
B:TYR202
|
3.9
|
20.4
|
1.0
|
|
CE3
|
B:TRP201
|
4.0
|
30.4
|
1.0
|
|
CG
|
B:PRO385
|
4.0
|
24.4
|
1.0
|
|
CG
|
B:ARG500
|
4.0
|
23.8
|
1.0
|
|
HG21
|
B:ILE499
|
4.1
|
23.7
|
1.0
|
|
CA
|
B:ARG500
|
4.1
|
24.1
|
1.0
|
|
CZ3
|
B:TRP201
|
4.1
|
29.9
|
1.0
|
|
HA
|
B:ARG500
|
4.1
|
28.9
|
1.0
|
|
CD
|
B:ARG500
|
4.2
|
25.1
|
1.0
|
|
HG2
|
B:PRO497
|
4.3
|
33.7
|
1.0
|
|
H
|
B:ILE499
|
4.3
|
24.2
|
1.0
|
|
HH22
|
B:ARG500
|
4.3
|
33.9
|
1.0
|
|
HB2
|
B:ARG500
|
4.3
|
27.3
|
1.0
|
|
CG
|
B:PRO497
|
4.6
|
28.1
|
1.0
|
|
N
|
B:ILE499
|
4.6
|
20.2
|
1.0
|
|
HG3
|
B:PRO385
|
4.7
|
29.2
|
1.0
|
|
C
|
B:ILE499
|
4.7
|
21.0
|
1.0
|
|
HD2
|
B:PRO385
|
4.7
|
27.7
|
1.0
|
|
C
|
B:PRO497
|
4.8
|
27.8
|
1.0
|
|
HD2
|
B:ARG500
|
4.8
|
30.1
|
1.0
|
|
HD3
|
B:ARG500
|
4.8
|
30.1
|
1.0
|
|
CA
|
B:PRO497
|
4.9
|
22.9
|
1.0
|
|
H
|
B:TYR498
|
4.9
|
25.9
|
1.0
|
|
O
|
B:HOH892
|
4.9
|
25.2
|
1.0
|
|
N
|
B:TYR498
|
4.9
|
21.6
|
1.0
|
|
HB3
|
B:TRP198
|
4.9
|
29.9
|
1.0
|
|
CB
|
B:ILE499
|
5.0
|
21.7
|
1.0
|
|
CD
|
B:PRO385
|
5.0
|
23.1
|
1.0
|
|
CA
|
B:ILE499
|
5.0
|
20.5
|
1.0
|
|
HG3
|
B:ARG500
|
5.0
|
28.5
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 6zpq
Go back to
Chlorine Binding Sites List in 6zpq
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl713
b:26.4
occ:1.00
|
HH
|
C:TYR202
|
2.2
|
31.1
|
1.0
|
|
HE
|
C:ARG500
|
2.3
|
34.2
|
1.0
|
|
HB3
|
C:ARG500
|
2.7
|
29.4
|
1.0
|
|
HH21
|
C:ARG500
|
2.8
|
38.7
|
1.0
|
|
HG22
|
C:ILE499
|
2.9
|
27.6
|
1.0
|
|
HB2
|
C:PRO497
|
2.9
|
32.3
|
1.0
|
|
H
|
C:ARG500
|
3.0
|
24.8
|
1.0
|
|
OH
|
C:TYR202
|
3.1
|
25.9
|
1.0
|
|
HB2
|
C:PRO385
|
3.1
|
31.1
|
1.0
|
|
HE1
|
C:TYR202
|
3.1
|
33.1
|
1.0
|
|
NE
|
C:ARG500
|
3.1
|
28.6
|
1.0
|
|
O
|
C:HOH1083
|
3.1
|
28.9
|
1.0
|
|
HE3
|
C:TRP201
|
3.2
|
38.0
|
1.0
|
|
HZ3
|
C:TRP201
|
3.3
|
42.3
|
1.0
|
|
HG2
|
C:PRO385
|
3.5
|
30.1
|
1.0
|
|
NH2
|
C:ARG500
|
3.5
|
32.3
|
1.0
|
|
CB
|
C:ARG500
|
3.6
|
24.6
|
1.0
|
|
N
|
C:ARG500
|
3.7
|
20.7
|
1.0
|
|
CG2
|
C:ILE499
|
3.7
|
23.0
|
1.0
|
|
HG2
|
C:ARG500
|
3.7
|
32.4
|
1.0
|
|
HG23
|
C:ILE499
|
3.7
|
27.6
|
1.0
|
|
HB3
|
C:PRO497
|
3.7
|
32.3
|
1.0
|
|
CB
|
C:PRO497
|
3.7
|
26.9
|
1.0
|
|
CB
|
C:PRO385
|
3.7
|
25.9
|
1.0
|
|
CE1
|
C:TYR202
|
3.8
|
27.6
|
1.0
|
|
HB3
|
C:PRO385
|
3.8
|
31.1
|
1.0
|
|
CZ
|
C:ARG500
|
3.8
|
35.4
|
1.0
|
|
CZ
|
C:TYR202
|
3.9
|
25.0
|
1.0
|
|
CE3
|
C:TRP201
|
3.9
|
31.7
|
1.0
|
|
CZ3
|
C:TRP201
|
3.9
|
35.3
|
1.0
|
|
CG
|
C:ARG500
|
4.0
|
27.1
|
1.0
|
|
HG21
|
C:ILE499
|
4.0
|
27.6
|
1.0
|
|
CA
|
C:ARG500
|
4.1
|
23.9
|
1.0
|
|
CG
|
C:PRO385
|
4.1
|
25.1
|
1.0
|
|
CD
|
C:ARG500
|
4.1
|
26.4
|
1.0
|
|
HA
|
C:ARG500
|
4.2
|
28.6
|
1.0
|
|
HG2
|
C:PRO497
|
4.2
|
40.2
|
1.0
|
|
H
|
C:ILE499
|
4.2
|
29.8
|
1.0
|
|
HB2
|
C:ARG500
|
4.3
|
29.4
|
1.0
|
|
HH22
|
C:ARG500
|
4.3
|
38.7
|
1.0
|
|
CG
|
C:PRO497
|
4.6
|
33.5
|
1.0
|
|
N
|
C:ILE499
|
4.6
|
24.9
|
1.0
|
|
C
|
C:ILE499
|
4.7
|
20.5
|
1.0
|
|
HD2
|
C:ARG500
|
4.7
|
31.7
|
1.0
|
|
C
|
C:PRO497
|
4.7
|
24.3
|
1.0
|
|
HG3
|
C:PRO385
|
4.7
|
30.1
|
1.0
|
|
HD3
|
C:ARG500
|
4.8
|
31.7
|
1.0
|
|
HD2
|
C:PRO385
|
4.9
|
31.3
|
1.0
|
|
CA
|
C:PRO497
|
4.9
|
25.7
|
1.0
|
|
H
|
C:TYR498
|
4.9
|
26.4
|
1.0
|
|
N
|
C:TYR498
|
4.9
|
22.1
|
1.0
|
|
CB
|
C:ILE499
|
4.9
|
26.9
|
1.0
|
|
HG3
|
C:ARG500
|
4.9
|
32.4
|
1.0
|
|
CA
|
C:ILE499
|
4.9
|
21.4
|
1.0
|
|
O
|
C:HOH961
|
5.0
|
27.0
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 6zpq
Go back to
Chlorine Binding Sites List in 6zpq
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl716
b:23.7
occ:1.00
|
HE
|
D:ARG500
|
2.3
|
34.5
|
1.0
|
|
HH
|
D:TYR202
|
2.3
|
29.1
|
1.0
|
|
HB3
|
D:ARG500
|
2.7
|
26.8
|
1.0
|
|
HH21
|
D:ARG500
|
2.9
|
36.0
|
1.0
|
|
HB2
|
D:PRO497
|
2.9
|
25.4
|
1.0
|
|
HG22
|
D:ILE499
|
3.0
|
22.2
|
1.0
|
|
H
|
D:ARG500
|
3.0
|
25.1
|
1.0
|
|
HB2
|
D:PRO385
|
3.0
|
29.5
|
1.0
|
|
O
|
D:HOH1100
|
3.1
|
21.1
|
1.0
|
|
OH
|
D:TYR202
|
3.1
|
24.3
|
1.0
|
|
HE1
|
D:TYR202
|
3.1
|
27.9
|
1.0
|
|
NE
|
D:ARG500
|
3.1
|
28.8
|
1.0
|
|
HE3
|
D:TRP201
|
3.3
|
32.9
|
1.0
|
|
HZ3
|
D:TRP201
|
3.3
|
31.7
|
1.0
|
|
HG2
|
D:PRO385
|
3.5
|
31.2
|
1.0
|
|
CB
|
D:ARG500
|
3.5
|
22.4
|
1.0
|
|
HG23
|
D:ILE499
|
3.5
|
22.2
|
1.0
|
|
HG2
|
D:ARG500
|
3.6
|
28.8
|
1.0
|
|
NH2
|
D:ARG500
|
3.6
|
30.0
|
1.0
|
|
HB3
|
D:PRO497
|
3.6
|
25.4
|
1.0
|
|
N
|
D:ARG500
|
3.6
|
20.9
|
1.0
|
|
CG2
|
D:ILE499
|
3.7
|
18.6
|
1.0
|
|
CB
|
D:PRO497
|
3.7
|
21.2
|
1.0
|
|
CB
|
D:PRO385
|
3.7
|
24.6
|
1.0
|
|
HB3
|
D:PRO385
|
3.7
|
29.5
|
1.0
|
|
CE1
|
D:TYR202
|
3.8
|
23.3
|
1.0
|
|
CZ
|
D:ARG500
|
3.8
|
32.7
|
1.0
|
|
CE3
|
D:TRP201
|
3.9
|
27.4
|
1.0
|
|
CZ
|
D:TYR202
|
3.9
|
24.5
|
1.0
|
|
CG
|
D:ARG500
|
3.9
|
24.0
|
1.0
|
|
CZ3
|
D:TRP201
|
3.9
|
26.5
|
1.0
|
|
CA
|
D:ARG500
|
4.0
|
21.6
|
1.0
|
|
HG21
|
D:ILE499
|
4.1
|
22.2
|
1.0
|
|
CG
|
D:PRO385
|
4.1
|
26.0
|
1.0
|
|
HA
|
D:ARG500
|
4.1
|
25.9
|
1.0
|
|
CD
|
D:ARG500
|
4.1
|
23.7
|
1.0
|
|
HG2
|
D:PRO497
|
4.2
|
33.0
|
1.0
|
|
HB2
|
D:ARG500
|
4.3
|
26.8
|
1.0
|
|
H
|
D:ILE499
|
4.3
|
23.1
|
1.0
|
|
HH22
|
D:ARG500
|
4.4
|
36.0
|
1.0
|
|
CG
|
D:PRO497
|
4.6
|
27.5
|
1.0
|
|
N
|
D:ILE499
|
4.6
|
19.3
|
1.0
|
|
C
|
D:ILE499
|
4.7
|
20.4
|
1.0
|
|
HD2
|
D:ARG500
|
4.7
|
28.4
|
1.0
|
|
H
|
D:TYR498
|
4.7
|
21.4
|
1.0
|
|
C
|
D:PRO497
|
4.7
|
23.0
|
1.0
|
|
HD2
|
D:PRO385
|
4.7
|
26.1
|
1.0
|
|
HG3
|
D:PRO385
|
4.7
|
31.2
|
1.0
|
|
HD3
|
D:ARG500
|
4.8
|
28.4
|
1.0
|
|
N
|
D:TYR498
|
4.8
|
17.8
|
1.0
|
|
CA
|
D:PRO497
|
4.8
|
24.5
|
1.0
|
|
HG3
|
D:ARG500
|
4.9
|
28.8
|
1.0
|
|
O
|
D:HOH960
|
4.9
|
21.7
|
1.0
|
|
CB
|
D:ILE499
|
4.9
|
20.8
|
1.0
|
|
CA
|
D:ILE499
|
5.0
|
16.5
|
1.0
|
|
HB3
|
D:TRP198
|
5.0
|
29.0
|
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: Mon Jul 29 18:10:12 2024
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