Chlorine in PDB 7l8n: Diadenylate Cyclase with Amp From Streptococcus Mutans
Enzymatic activity of Diadenylate Cyclase with Amp From Streptococcus Mutans
All present enzymatic activity of Diadenylate Cyclase with Amp From Streptococcus Mutans:
2.7.7.85;
Protein crystallography data
The structure of Diadenylate Cyclase with Amp From Streptococcus Mutans, PDB code: 7l8n
was solved by
Z.Hua,
W.Hui,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.97 /
1.94
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
76.36,
84.59,
100.24,
90,
90,
90
|
R / Rfree (%)
|
16.1 /
20.7
|
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Diadenylate Cyclase with Amp From Streptococcus Mutans
(pdb code 7l8n). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the
Diadenylate Cyclase with Amp From Streptococcus Mutans, PDB code: 7l8n:
Jump to Chlorine binding site number:
1;
2;
Chlorine binding site 1 out
of 2 in 7l8n
Go back to
Chlorine Binding Sites List in 7l8n
Chlorine binding site 1 out
of 2 in the Diadenylate Cyclase with Amp From Streptococcus Mutans
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Diadenylate Cyclase with Amp From Streptococcus Mutans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl302
b:43.4
occ:1.00
|
H
|
B:SER251
|
2.8
|
37.0
|
1.0
|
HA
|
B:LEU250
|
2.8
|
36.2
|
1.0
|
O
|
B:HOH408
|
3.2
|
35.3
|
1.0
|
N
|
B:SER251
|
3.5
|
30.8
|
1.0
|
HD23
|
B:LEU250
|
3.6
|
42.3
|
1.0
|
CA
|
B:LEU250
|
3.7
|
30.1
|
1.0
|
HB3
|
B:ALA254
|
3.8
|
35.2
|
1.0
|
HB2
|
B:ALA254
|
3.8
|
35.2
|
1.0
|
O
|
B:ASP249
|
3.9
|
33.2
|
1.0
|
HB3
|
B:SER251
|
4.0
|
32.9
|
1.0
|
HB1
|
B:ALA254
|
4.1
|
35.2
|
1.0
|
CB
|
B:ALA254
|
4.1
|
29.3
|
1.0
|
C
|
B:LEU250
|
4.1
|
33.9
|
1.0
|
HB3
|
B:LEU250
|
4.5
|
32.7
|
1.0
|
CD2
|
B:LEU250
|
4.5
|
35.2
|
1.0
|
CB
|
B:LEU250
|
4.6
|
27.2
|
1.0
|
N
|
B:LEU250
|
4.6
|
27.9
|
1.0
|
CB
|
B:SER251
|
4.6
|
27.3
|
1.0
|
OG
|
B:SER251
|
4.6
|
25.7
|
1.0
|
C
|
B:ASP249
|
4.6
|
37.1
|
1.0
|
CA
|
B:SER251
|
4.7
|
31.5
|
1.0
|
HD22
|
B:LEU250
|
4.8
|
42.3
|
1.0
|
HG
|
B:LEU250
|
5.0
|
31.9
|
1.0
|
CG
|
B:LEU250
|
5.0
|
26.5
|
1.0
|
|
Chlorine binding site 2 out
of 2 in 7l8n
Go back to
Chlorine Binding Sites List in 7l8n
Chlorine binding site 2 out
of 2 in the Diadenylate Cyclase with Amp From Streptococcus Mutans
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Diadenylate Cyclase with Amp From Streptococcus Mutans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl303
b:46.5
occ:1.00
|
HE2
|
B:HIS214
|
1.9
|
38.3
|
1.0
|
HG
|
B:SER239
|
2.4
|
40.5
|
1.0
|
NE2
|
B:HIS214
|
2.7
|
31.8
|
1.0
|
OG
|
B:SER239
|
2.7
|
33.7
|
1.0
|
O
|
B:ALA237
|
2.8
|
22.0
|
1.0
|
HB2
|
B:SER239
|
2.9
|
32.0
|
1.0
|
HB2
|
B:SER232
|
3.1
|
30.3
|
1.0
|
CB
|
B:SER239
|
3.3
|
26.6
|
1.0
|
HB3
|
B:ALA237
|
3.3
|
31.5
|
1.0
|
H
|
B:SER232
|
3.4
|
29.1
|
1.0
|
C
|
B:ALA237
|
3.4
|
23.6
|
1.0
|
CD2
|
B:HIS214
|
3.5
|
37.5
|
1.0
|
H
|
B:SER239
|
3.5
|
26.0
|
1.0
|
HD2
|
B:HIS214
|
3.5
|
45.1
|
1.0
|
HD2
|
B:HIS248
|
3.5
|
63.8
|
1.0
|
N
|
B:SER239
|
3.6
|
21.6
|
1.0
|
HB
|
B:VAL230
|
3.7
|
29.9
|
1.0
|
HG12
|
B:VAL230
|
3.7
|
29.9
|
1.0
|
HB1
|
B:ALA237
|
3.7
|
31.5
|
1.0
|
CE1
|
B:HIS214
|
3.7
|
37.0
|
1.0
|
CB
|
B:SER232
|
3.8
|
25.2
|
1.0
|
N
|
B:SER232
|
3.8
|
24.2
|
1.0
|
HB3
|
B:SER232
|
3.9
|
30.3
|
1.0
|
C
|
B:ILE238
|
3.9
|
26.5
|
1.0
|
CB
|
B:ALA237
|
3.9
|
26.2
|
1.0
|
O
|
B:VAL230
|
3.9
|
21.7
|
1.0
|
HA
|
B:ILE238
|
3.9
|
27.4
|
1.0
|
HE1
|
B:HIS214
|
3.9
|
44.5
|
1.0
|
N
|
B:ILE238
|
4.1
|
22.5
|
1.0
|
CA
|
B:SER239
|
4.1
|
22.7
|
1.0
|
HA
|
B:VAL231
|
4.1
|
21.4
|
1.0
|
HB3
|
B:SER239
|
4.1
|
32.0
|
1.0
|
CA
|
B:ILE238
|
4.2
|
22.8
|
1.0
|
CD2
|
B:HIS248
|
4.2
|
53.2
|
1.0
|
CA
|
B:ALA237
|
4.2
|
26.3
|
1.0
|
CG1
|
B:VAL230
|
4.3
|
24.9
|
1.0
|
CA
|
B:SER232
|
4.3
|
21.8
|
1.0
|
HZ
|
B:PHE246
|
4.4
|
39.4
|
1.0
|
HE1
|
B:PHE210
|
4.4
|
76.2
|
1.0
|
H
|
B:ASP249
|
4.4
|
34.9
|
1.0
|
C
|
B:VAL230
|
4.4
|
21.4
|
1.0
|
HG11
|
B:VAL230
|
4.4
|
29.9
|
1.0
|
CB
|
B:VAL230
|
4.4
|
24.9
|
1.0
|
O
|
B:ILE238
|
4.5
|
23.4
|
1.0
|
HA
|
B:SER232
|
4.5
|
26.2
|
1.0
|
NE2
|
B:HIS248
|
4.5
|
59.7
|
1.0
|
C
|
B:VAL231
|
4.5
|
20.3
|
1.0
|
HA
|
B:SER239
|
4.6
|
27.3
|
1.0
|
CA
|
B:VAL231
|
4.6
|
17.8
|
1.0
|
H
|
B:ILE238
|
4.7
|
27.1
|
1.0
|
CG
|
B:HIS214
|
4.7
|
37.4
|
1.0
|
HB2
|
B:ALA237
|
4.8
|
31.5
|
1.0
|
ND1
|
B:HIS214
|
4.8
|
41.9
|
1.0
|
N
|
B:VAL231
|
4.8
|
17.1
|
1.0
|
N
|
B:ALA237
|
4.9
|
23.3
|
1.0
|
H
|
B:ALA237
|
4.9
|
28.1
|
1.0
|
|
Reference:
Z.Hua,
W.Hui.
Diadenylate Cyclase with Amp From Streptococcus Mutans To Be Published.
Page generated: Mon Jul 29 23:55:10 2024
|