Chlorine in PDB 6f9v: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.
Enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.
All present enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.:
3.4.15.1;
Protein crystallography data
The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat., PDB code: 6f9v
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)
|
21.97 /
1.69
|
|
Space group
|
P 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
73.224,
77.215,
83.107,
88.36,
64.20,
75.29
|
|
R / Rfree (%)
|
18.3 /
21.2
|
Other elements in 6f9v:
The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat. also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.
(pdb code 6f9v). 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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat., PDB code: 6f9v:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 6f9v
Go back to
Chlorine Binding Sites List in 6f9v
Chlorine binding site 1 out
of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.
 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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl703
b:22.9
occ:1.00
|
HH
|
A:TYR202
|
2.3
|
27.2
|
1.0
|
|
HE
|
A:ARG500
|
2.3
|
28.1
|
1.0
|
|
HH21
|
A:ARG500
|
2.7
|
31.5
|
1.0
|
|
HB3
|
A:ARG500
|
2.7
|
24.5
|
1.0
|
|
HB2
|
A:PRO497
|
2.9
|
27.9
|
1.0
|
|
OH
|
A:TYR202
|
3.0
|
22.7
|
1.0
|
|
H
|
A:ARG500
|
3.1
|
22.1
|
1.0
|
|
HB2
|
A:PRO385
|
3.1
|
33.6
|
1.0
|
|
O
|
A:HOH1128
|
3.1
|
24.4
|
1.0
|
|
HE2
|
A:TYR202
|
3.1
|
29.6
|
1.0
|
|
NE
|
A:ARG500
|
3.1
|
23.4
|
1.0
|
|
HE3
|
A:TRP201
|
3.2
|
35.8
|
1.0
|
|
HG2
|
A:PRO385
|
3.2
|
27.0
|
1.0
|
|
HZ3
|
A:TRP201
|
3.3
|
40.1
|
1.0
|
|
HG22
|
A:ILE499
|
3.3
|
24.6
|
1.0
|
|
NH2
|
A:ARG500
|
3.4
|
26.2
|
1.0
|
|
CB
|
A:ARG500
|
3.6
|
20.4
|
1.0
|
|
HG2
|
A:ARG500
|
3.7
|
26.6
|
1.0
|
|
N
|
A:ARG500
|
3.7
|
18.4
|
1.0
|
|
CB
|
A:PRO497
|
3.7
|
23.2
|
1.0
|
|
HG23
|
A:ILE499
|
3.8
|
24.6
|
1.0
|
|
CB
|
A:PRO385
|
3.8
|
28.0
|
1.0
|
|
CZ
|
A:ARG500
|
3.8
|
29.3
|
1.0
|
|
HB3
|
A:PRO497
|
3.8
|
27.9
|
1.0
|
|
CE2
|
A:TYR202
|
3.8
|
24.7
|
1.0
|
|
CE3
|
A:TRP201
|
3.9
|
29.8
|
1.0
|
|
CZ
|
A:TYR202
|
3.9
|
23.1
|
1.0
|
|
HB3
|
A:PRO385
|
3.9
|
33.6
|
1.0
|
|
CZ3
|
A:TRP201
|
3.9
|
33.4
|
1.0
|
|
CG
|
A:PRO385
|
3.9
|
22.5
|
1.0
|
|
CG2
|
A:ILE499
|
4.0
|
20.5
|
1.0
|
|
CG
|
A:ARG500
|
4.0
|
22.2
|
1.0
|
|
CA
|
A:ARG500
|
4.1
|
19.3
|
1.0
|
|
HG2
|
A:PRO497
|
4.1
|
28.9
|
1.0
|
|
HA
|
A:ARG500
|
4.1
|
23.2
|
1.0
|
|
HH22
|
A:ARG500
|
4.2
|
31.5
|
1.0
|
|
CD
|
A:ARG500
|
4.2
|
21.7
|
1.0
|
|
HB2
|
A:ARG500
|
4.3
|
24.5
|
1.0
|
|
HG21
|
A:ILE499
|
4.5
|
24.6
|
1.0
|
|
HD2
|
A:PRO385
|
4.5
|
26.3
|
1.0
|
|
CG
|
A:PRO497
|
4.5
|
24.1
|
1.0
|
|
H
|
A:ILE499
|
4.5
|
26.1
|
1.0
|
|
HG3
|
A:PRO385
|
4.6
|
27.0
|
1.0
|
|
C
|
A:ILE499
|
4.7
|
18.9
|
1.0
|
|
C
|
A:PRO497
|
4.8
|
23.2
|
1.0
|
|
HD3
|
A:ARG500
|
4.8
|
26.0
|
1.0
|
|
N
|
A:ILE499
|
4.8
|
21.7
|
1.0
|
|
HD2
|
A:ARG500
|
4.8
|
26.0
|
1.0
|
|
CD
|
A:PRO385
|
4.8
|
21.9
|
1.0
|
|
CA
|
A:PRO497
|
4.9
|
21.1
|
1.0
|
|
O
|
A:HOH1021
|
5.0
|
21.3
|
1.0
|
|
O
|
A:PRO497
|
5.0
|
21.4
|
1.0
|
|
HG3
|
A:ARG500
|
5.0
|
26.6
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 6f9v
Go back to
Chlorine Binding Sites List in 6f9v
Chlorine binding site 2 out
of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.
 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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl704
b:26.9
occ:1.00
|
H
|
A:GLY382
|
2.3
|
28.9
|
1.0
|
|
HA
|
A:PRO385
|
2.9
|
27.6
|
1.0
|
|
HB3
|
A:ARG381
|
3.1
|
35.8
|
1.0
|
|
N11
|
A:D0Z702
|
3.1
|
25.8
|
1.0
|
|
N
|
A:GLY382
|
3.1
|
24.1
|
1.0
|
|
HD3
|
A:ARG381
|
3.1
|
40.2
|
1.0
|
|
O
|
A:HOH1122
|
3.2
|
31.6
|
1.0
|
|
H102
|
A:D0Z702
|
3.2
|
32.9
|
1.0
|
|
HD2
|
A:HIS388
|
3.2
|
27.4
|
1.0
|
|
H11
|
A:EDO718
|
3.4
|
58.0
|
1.0
|
|
H111
|
A:D0Z702
|
3.5
|
31.0
|
1.0
|
|
HA3
|
A:GLY382
|
3.5
|
30.6
|
1.0
|
|
HB2
|
A:HIS388
|
3.6
|
27.0
|
1.0
|
|
H112
|
A:D0Z702
|
3.6
|
31.0
|
1.0
|
|
HG3
|
A:PRO385
|
3.6
|
27.0
|
1.0
|
|
C10
|
A:D0Z702
|
3.7
|
27.4
|
1.0
|
|
CA
|
A:PRO385
|
3.8
|
23.0
|
1.0
|
|
HA
|
A:ARG381
|
3.8
|
31.8
|
1.0
|
|
CA
|
A:GLY382
|
3.9
|
25.5
|
1.0
|
|
CD2
|
A:HIS388
|
3.9
|
22.9
|
1.0
|
|
CB
|
A:ARG381
|
3.9
|
29.8
|
1.0
|
|
HB3
|
A:PRO385
|
4.0
|
33.6
|
1.0
|
|
CD
|
A:ARG381
|
4.0
|
33.5
|
1.0
|
|
HH11
|
A:ARG381
|
4.0
|
40.4
|
1.0
|
|
H101
|
A:D0Z702
|
4.0
|
32.9
|
1.0
|
|
C
|
A:ARG381
|
4.1
|
22.0
|
1.0
|
|
CA
|
A:ARG381
|
4.2
|
26.5
|
1.0
|
|
N
|
A:PRO385
|
4.2
|
21.4
|
1.0
|
|
CB
|
A:PRO385
|
4.3
|
28.0
|
1.0
|
|
NE
|
A:ARG381
|
4.3
|
31.4
|
1.0
|
|
NH1
|
A:ARG381
|
4.3
|
33.6
|
1.0
|
|
CG
|
A:PRO385
|
4.3
|
22.5
|
1.0
|
|
CB
|
A:HIS388
|
4.4
|
22.5
|
1.0
|
|
CG
|
A:HIS388
|
4.4
|
23.5
|
1.0
|
|
O
|
A:ASN384
|
4.4
|
24.9
|
1.0
|
|
C1
|
A:EDO718
|
4.4
|
48.3
|
1.0
|
|
CZ
|
A:ARG381
|
4.4
|
29.3
|
1.0
|
|
O
|
A:HOH919
|
4.4
|
26.4
|
1.0
|
|
O
|
A:GLY382
|
4.5
|
24.5
|
1.0
|
|
C
|
A:ASN384
|
4.5
|
25.0
|
1.0
|
|
CG
|
A:ARG381
|
4.6
|
31.2
|
1.0
|
|
C
|
A:GLY382
|
4.6
|
27.4
|
1.0
|
|
HB3
|
A:HIS388
|
4.6
|
27.0
|
1.0
|
|
HB2
|
A:ARG381
|
4.7
|
35.8
|
1.0
|
|
HA2
|
A:GLY382
|
4.7
|
30.6
|
1.0
|
|
HE
|
A:ARG381
|
4.7
|
37.6
|
1.0
|
|
HH12
|
A:ARG381
|
4.7
|
40.4
|
1.0
|
|
HD2
|
A:ARG381
|
4.7
|
40.2
|
1.0
|
|
HO1
|
A:EDO718
|
4.7
|
67.8
|
1.0
|
|
CD
|
A:PRO385
|
4.8
|
21.9
|
1.0
|
|
HD3
|
A:PRO385
|
4.8
|
26.3
|
1.0
|
|
O1
|
A:EDO718
|
4.8
|
56.5
|
1.0
|
|
C
|
A:PRO385
|
4.9
|
24.3
|
1.0
|
|
H21
|
A:EDO718
|
4.9
|
59.1
|
1.0
|
|
O
|
A:PRO385
|
4.9
|
23.7
|
1.0
|
|
NE2
|
A:HIS388
|
4.9
|
25.9
|
1.0
|
|
C09
|
A:D0Z702
|
5.0
|
34.5
|
1.0
|
|
H
|
A:HIS388
|
5.0
|
25.9
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 6f9v
Go back to
Chlorine Binding Sites List in 6f9v
Chlorine binding site 3 out
of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.
 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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl703
b:30.6
occ:1.00
|
HH
|
B:TYR202
|
2.3
|
36.1
|
1.0
|
|
HE
|
B:ARG500
|
2.4
|
29.3
|
1.0
|
|
HB3
|
B:ARG500
|
2.8
|
26.4
|
1.0
|
|
HH21
|
B:ARG500
|
2.8
|
34.0
|
1.0
|
|
HB2
|
B:PRO497
|
2.9
|
32.7
|
1.0
|
|
O
|
B:HOH1043
|
3.0
|
32.5
|
1.0
|
|
OH
|
B:TYR202
|
3.1
|
30.1
|
1.0
|
|
H
|
B:ARG500
|
3.1
|
30.6
|
1.0
|
|
HB2
|
B:PRO385
|
3.2
|
33.6
|
1.0
|
|
HE1
|
B:TYR202
|
3.2
|
45.5
|
1.0
|
|
HE3
|
B:TRP201
|
3.2
|
39.1
|
1.0
|
|
HZ3
|
B:TRP201
|
3.2
|
41.8
|
1.0
|
|
NE
|
B:ARG500
|
3.2
|
24.4
|
1.0
|
|
HG22
|
B:ILE499
|
3.3
|
31.3
|
1.0
|
|
HG2
|
B:PRO385
|
3.4
|
43.2
|
1.0
|
|
NH2
|
B:ARG500
|
3.5
|
28.3
|
1.0
|
|
CB
|
B:ARG500
|
3.6
|
22.0
|
1.0
|
|
CB
|
B:PRO497
|
3.7
|
27.3
|
1.0
|
|
HB3
|
B:PRO497
|
3.7
|
32.7
|
1.0
|
|
HG23
|
B:ILE499
|
3.7
|
31.3
|
1.0
|
|
HG2
|
B:ARG500
|
3.7
|
28.2
|
1.0
|
|
N
|
B:ARG500
|
3.7
|
25.5
|
1.0
|
|
CB
|
B:PRO385
|
3.8
|
28.0
|
1.0
|
|
CE3
|
B:TRP201
|
3.8
|
32.6
|
1.0
|
|
CE1
|
B:TYR202
|
3.8
|
37.9
|
1.0
|
|
CZ
|
B:ARG500
|
3.9
|
25.8
|
1.0
|
|
CZ3
|
B:TRP201
|
3.9
|
34.8
|
1.0
|
|
CZ
|
B:TYR202
|
3.9
|
31.8
|
1.0
|
|
CG2
|
B:ILE499
|
3.9
|
26.1
|
1.0
|
|
HB3
|
B:PRO385
|
3.9
|
33.6
|
1.0
|
|
CG
|
B:ARG500
|
4.0
|
23.5
|
1.0
|
|
CG
|
B:PRO385
|
4.1
|
36.0
|
1.0
|
|
HG2
|
B:PRO497
|
4.1
|
35.3
|
1.0
|
|
CA
|
B:ARG500
|
4.1
|
23.4
|
1.0
|
|
HA
|
B:ARG500
|
4.2
|
28.1
|
1.0
|
|
CD
|
B:ARG500
|
4.3
|
23.4
|
1.0
|
|
HH22
|
B:ARG500
|
4.3
|
34.0
|
1.0
|
|
HB2
|
B:ARG500
|
4.4
|
26.4
|
1.0
|
|
H
|
B:ILE499
|
4.4
|
29.5
|
1.0
|
|
HG21
|
B:ILE499
|
4.4
|
31.3
|
1.0
|
|
CG
|
B:PRO497
|
4.5
|
29.4
|
1.0
|
|
HD2
|
B:PRO385
|
4.6
|
42.9
|
1.0
|
|
N
|
B:ILE499
|
4.7
|
24.6
|
1.0
|
|
C
|
B:ILE499
|
4.7
|
19.6
|
1.0
|
|
HG3
|
B:PRO385
|
4.8
|
43.2
|
1.0
|
|
C
|
B:PRO497
|
4.8
|
28.4
|
1.0
|
|
HD2
|
B:ARG500
|
4.8
|
28.1
|
1.0
|
|
O
|
B:HOH951
|
4.8
|
31.4
|
1.0
|
|
HD3
|
B:ARG500
|
4.9
|
28.1
|
1.0
|
|
CA
|
B:PRO497
|
4.9
|
21.1
|
1.0
|
|
CD
|
B:PRO385
|
4.9
|
35.8
|
1.0
|
|
O
|
B:PRO497
|
5.0
|
23.9
|
1.0
|
|
HG3
|
B:ARG500
|
5.0
|
28.2
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 6f9v
Go back to
Chlorine Binding Sites List in 6f9v
Chlorine binding site 4 out
of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat.
 Mono view
 Stereo pair view
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A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Sampatrilat. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl704
b:35.0
occ:1.00
|
H111
|
B:D0Z702
|
2.2
|
37.5
|
1.0
|
|
H
|
B:GLY382
|
2.4
|
33.7
|
1.0
|
|
HA
|
B:PRO385
|
2.8
|
35.6
|
1.0
|
|
HB3
|
B:ARG381
|
2.9
|
48.5
|
1.0
|
|
N11
|
B:D0Z702
|
3.0
|
31.2
|
1.0
|
|
O
|
B:HOH1084
|
3.1
|
41.1
|
1.0
|
|
H12
|
B:EDO711
|
3.1
|
57.1
|
1.0
|
|
HD2
|
B:HIS388
|
3.2
|
42.7
|
1.0
|
|
N
|
B:GLY382
|
3.3
|
28.1
|
1.0
|
|
HD3
|
B:ARG381
|
3.4
|
53.6
|
1.0
|
|
HG3
|
B:PRO385
|
3.4
|
43.2
|
1.0
|
|
HB2
|
B:HIS388
|
3.6
|
35.1
|
1.0
|
|
H112
|
B:D0Z702
|
3.6
|
37.5
|
1.0
|
|
CA
|
B:PRO385
|
3.6
|
29.7
|
1.0
|
|
HA3
|
B:GLY382
|
3.8
|
42.9
|
1.0
|
|
H102
|
B:D0Z702
|
3.8
|
46.7
|
1.0
|
|
C10
|
B:D0Z702
|
3.8
|
38.9
|
1.0
|
|
CB
|
B:ARG381
|
3.8
|
40.4
|
1.0
|
|
HA
|
B:ARG381
|
3.8
|
37.8
|
1.0
|
|
HB3
|
B:PRO385
|
3.8
|
33.6
|
1.0
|
|
H101
|
B:D0Z702
|
3.8
|
46.7
|
1.0
|
|
CD2
|
B:HIS388
|
3.9
|
35.5
|
1.0
|
|
CA
|
B:GLY382
|
4.1
|
35.7
|
1.0
|
|
N
|
B:PRO385
|
4.1
|
37.2
|
1.0
|
|
CB
|
B:PRO385
|
4.1
|
28.0
|
1.0
|
|
CG
|
B:PRO385
|
4.1
|
36.0
|
1.0
|
|
C1
|
B:EDO711
|
4.1
|
47.6
|
1.0
|
|
CA
|
B:ARG381
|
4.1
|
31.5
|
1.0
|
|
CD
|
B:ARG381
|
4.2
|
44.6
|
1.0
|
|
HH11
|
B:ARG381
|
4.2
|
51.8
|
1.0
|
|
C
|
B:ARG381
|
4.2
|
37.9
|
1.0
|
|
H11
|
B:EDO711
|
4.3
|
57.1
|
1.0
|
|
CB
|
B:HIS388
|
4.3
|
29.2
|
1.0
|
|
O
|
B:HOH907
|
4.4
|
27.9
|
1.0
|
|
NE
|
B:ARG381
|
4.4
|
46.4
|
1.0
|
|
O
|
B:ASN384
|
4.4
|
33.9
|
1.0
|
|
NH1
|
B:ARG381
|
4.4
|
43.2
|
1.0
|
|
C
|
B:ASN384
|
4.4
|
38.1
|
1.0
|
|
CG
|
B:HIS388
|
4.4
|
25.9
|
1.0
|
|
HB2
|
B:ARG381
|
4.4
|
48.5
|
1.0
|
|
H22
|
B:EDO711
|
4.4
|
58.2
|
1.0
|
|
CZ
|
B:ARG381
|
4.5
|
46.3
|
1.0
|
|
HB3
|
B:HIS388
|
4.5
|
35.1
|
1.0
|
|
CG
|
B:ARG381
|
4.5
|
33.2
|
1.0
|
|
CD
|
B:PRO385
|
4.6
|
35.8
|
1.0
|
|
HD3
|
B:PRO385
|
4.6
|
42.9
|
1.0
|
|
O
|
B:GLY382
|
4.7
|
36.5
|
1.0
|
|
C
|
B:PRO385
|
4.8
|
29.8
|
1.0
|
|
HH12
|
B:ARG381
|
4.8
|
51.8
|
1.0
|
|
C
|
B:GLY382
|
4.8
|
27.0
|
1.0
|
|
O
|
B:PRO385
|
4.8
|
28.0
|
1.0
|
|
HE
|
B:ARG381
|
4.8
|
55.7
|
1.0
|
|
HA2
|
B:GLY382
|
4.9
|
42.9
|
1.0
|
|
H
|
B:HIS388
|
4.9
|
33.8
|
1.0
|
|
C2
|
B:EDO711
|
4.9
|
48.5
|
1.0
|
|
HG2
|
B:PRO385
|
4.9
|
43.2
|
1.0
|
|
HD2
|
B:ARG381
|
5.0
|
53.6
|
1.0
|
|
HG3
|
B:ARG381
|
5.0
|
39.8
|
1.0
|
|
HO1
|
B:EDO711
|
5.0
|
62.5
|
1.0
|
|
Reference:
G.E.Cozier,
S.L.Schwager,
R.K.Sharma,
K.Chibale,
E.D.Sturrock,
K.R.Acharya.
Crystal Structures of Sampatrilat and Sampatrilat-Asp in Complex with Human Ace - A Molecular Basis For Domain Selectivity. Febs J. V. 285 1477 2018.
ISSN: ISSN 1742-4658
PubMed: 29476645
DOI: 10.1111/FEBS.14421
Page generated: Sat Jul 27 23:06:10 2024
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