Chlorine in PDB 6ub9: Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form
Enzymatic activity of Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form
All present enzymatic activity of Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form:
4.2.1.20;
Protein crystallography data
The structure of Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form, PDB code: 6ub9
was solved by
C.Chang,
K.Michalska,
N.I.Maltseva,
R.Jedrzejczak,
P.Mccarren,
P.P.Nag,
A.Joachimiak,
K.Satchell,
Center For Structural Genomics Of Infectiousdiseases (Csgid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.89 /
2.78
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
135.373,
159.619,
164.932,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.9 /
21
|
Other elements in 6ub9:
The structure of Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form
(pdb code 6ub9). 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 Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form, PDB code: 6ub9:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 6ub9
Go back to
Chlorine Binding Sites List in 6ub9
Chlorine binding site 1 out
of 4 in the Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form
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 Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl502
b:40.5
occ:1.00
|
CL1
|
B:H9V502
|
0.0
|
40.5
|
1.0
|
C10
|
B:H9V502
|
1.7
|
38.1
|
1.0
|
C9
|
B:H9V502
|
2.7
|
37.9
|
1.0
|
C11
|
B:H9V502
|
2.7
|
37.2
|
1.0
|
CE2
|
B:PHE211
|
3.3
|
24.1
|
1.0
|
CD2
|
B:PHE211
|
3.4
|
25.1
|
1.0
|
CB
|
B:PHE202
|
3.5
|
31.5
|
1.0
|
CZ
|
B:PHE211
|
3.5
|
23.5
|
1.0
|
CG
|
B:PHE211
|
3.6
|
21.5
|
1.0
|
CG
|
B:PHE202
|
3.6
|
31.6
|
1.0
|
CE1
|
B:PHE211
|
3.7
|
24.5
|
1.0
|
CD1
|
B:PHE211
|
3.7
|
21.3
|
1.0
|
CD2
|
B:TYR200
|
3.8
|
34.0
|
1.0
|
CE2
|
B:TYR200
|
3.9
|
34.7
|
1.0
|
C8
|
B:H9V502
|
4.0
|
37.9
|
1.0
|
C12
|
B:H9V502
|
4.0
|
38.2
|
1.0
|
CD2
|
B:PHE202
|
4.0
|
31.4
|
1.0
|
CD1
|
B:PHE202
|
4.1
|
32.0
|
1.0
|
CD
|
B:PRO208
|
4.2
|
26.4
|
1.0
|
CG
|
B:TYR200
|
4.3
|
33.6
|
1.0
|
CZ
|
B:TYR200
|
4.4
|
35.0
|
1.0
|
CB
|
B:PHE211
|
4.4
|
23.6
|
1.0
|
C7
|
B:H9V502
|
4.5
|
39.5
|
1.0
|
CZ3
|
B:TRP191
|
4.6
|
27.7
|
1.0
|
CA
|
B:PHE202
|
4.7
|
32.1
|
1.0
|
CG
|
B:PRO208
|
4.8
|
26.9
|
1.0
|
CE2
|
B:PHE202
|
4.8
|
31.3
|
1.0
|
CD1
|
B:TYR200
|
4.8
|
34.3
|
1.0
|
CE1
|
B:TYR200
|
4.9
|
33.7
|
1.0
|
CE1
|
B:PHE202
|
4.9
|
31.9
|
1.0
|
F2
|
B:H9V502
|
4.9
|
39.1
|
1.0
|
O
|
B:TYR200
|
5.0
|
34.6
|
1.0
|
N
|
B:PHE202
|
5.0
|
30.4
|
1.0
|
CB
|
B:TYR200
|
5.0
|
33.3
|
1.0
|
F1
|
B:H9V502
|
5.0
|
38.1
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 6ub9
Go back to
Chlorine Binding Sites List in 6ub9
Chlorine binding site 2 out
of 4 in the Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form
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 Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cl502
b:59.1
occ:0.76
|
CL1
|
D:H9V502
|
0.0
|
59.1
|
0.8
|
C10
|
D:H9V502
|
1.7
|
60.6
|
0.8
|
C11
|
D:H9V502
|
2.7
|
60.7
|
0.8
|
C9
|
D:H9V502
|
2.7
|
60.7
|
0.8
|
CE2
|
D:PHE211
|
3.3
|
28.5
|
1.0
|
CD2
|
D:PHE211
|
3.3
|
27.6
|
1.0
|
CG
|
D:PHE202
|
3.5
|
42.8
|
1.0
|
CZ
|
D:PHE211
|
3.5
|
27.6
|
1.0
|
CB
|
D:PHE202
|
3.6
|
38.2
|
1.0
|
CG
|
D:PHE211
|
3.7
|
26.8
|
1.0
|
CD1
|
D:PHE202
|
3.7
|
44.5
|
1.0
|
CD2
|
D:TYR200
|
3.7
|
30.2
|
1.0
|
CE1
|
D:PHE211
|
3.9
|
27.8
|
1.0
|
CE2
|
D:TYR200
|
3.9
|
28.5
|
1.0
|
CD1
|
D:PHE211
|
3.9
|
27.4
|
1.0
|
C12
|
D:H9V502
|
4.0
|
60.3
|
0.8
|
CD2
|
D:PHE202
|
4.0
|
43.4
|
1.0
|
C8
|
D:H9V502
|
4.0
|
60.0
|
0.8
|
CD
|
D:PRO208
|
4.2
|
29.7
|
1.0
|
CG
|
D:TYR200
|
4.3
|
28.8
|
1.0
|
CE1
|
D:PHE202
|
4.3
|
45.0
|
1.0
|
CZ3
|
D:TRP191
|
4.4
|
24.4
|
1.0
|
CB
|
D:PHE211
|
4.5
|
27.5
|
1.0
|
CZ
|
D:TYR200
|
4.6
|
33.4
|
1.0
|
C7
|
D:H9V502
|
4.6
|
59.8
|
0.8
|
CE2
|
D:PHE202
|
4.6
|
44.4
|
1.0
|
CA
|
D:PHE202
|
4.7
|
33.0
|
1.0
|
CZ
|
D:PHE202
|
4.8
|
45.2
|
1.0
|
CG
|
D:PRO208
|
4.8
|
27.8
|
1.0
|
CB
|
D:TYR200
|
4.8
|
28.9
|
1.0
|
CD1
|
D:TYR200
|
4.9
|
29.6
|
1.0
|
F1
|
D:H9V502
|
4.9
|
60.8
|
0.8
|
CE3
|
D:TRP191
|
5.0
|
24.6
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 6ub9
Go back to
Chlorine Binding Sites List in 6ub9
Chlorine binding site 3 out
of 4 in the Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form
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 Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Cl502
b:43.1
occ:1.00
|
CL1
|
F:H9V502
|
0.0
|
43.1
|
1.0
|
C10
|
F:H9V502
|
1.7
|
43.8
|
1.0
|
C9
|
F:H9V502
|
2.7
|
43.2
|
1.0
|
C11
|
F:H9V502
|
2.7
|
43.8
|
1.0
|
CD2
|
F:PHE211
|
3.4
|
25.9
|
1.0
|
CE2
|
F:PHE211
|
3.4
|
24.6
|
1.0
|
CB
|
F:PHE202
|
3.4
|
33.8
|
1.0
|
CG
|
F:PHE202
|
3.5
|
33.5
|
1.0
|
CG
|
F:PHE211
|
3.6
|
26.8
|
1.0
|
CZ
|
F:PHE211
|
3.7
|
26.9
|
1.0
|
CD1
|
F:PHE211
|
3.8
|
24.4
|
1.0
|
CD2
|
F:PHE202
|
3.8
|
32.9
|
1.0
|
CE1
|
F:PHE211
|
3.8
|
23.6
|
1.0
|
CD2
|
F:TYR200
|
3.9
|
34.5
|
1.0
|
C8
|
F:H9V502
|
4.0
|
44.6
|
1.0
|
C12
|
F:H9V502
|
4.0
|
44.5
|
1.0
|
CD
|
F:PRO208
|
4.0
|
31.8
|
1.0
|
CE2
|
F:TYR200
|
4.1
|
35.1
|
1.0
|
CD1
|
F:PHE202
|
4.1
|
32.3
|
1.0
|
CB
|
F:PHE211
|
4.4
|
22.9
|
1.0
|
CG
|
F:TYR200
|
4.5
|
32.6
|
1.0
|
C7
|
F:H9V502
|
4.6
|
45.8
|
1.0
|
CE2
|
F:PHE202
|
4.6
|
32.7
|
1.0
|
CZ3
|
F:TRP191
|
4.6
|
29.1
|
1.0
|
CG
|
F:PRO208
|
4.7
|
32.6
|
1.0
|
CZ
|
F:TYR200
|
4.8
|
34.8
|
1.0
|
CA
|
F:PHE202
|
4.8
|
33.8
|
1.0
|
CE1
|
F:PHE202
|
4.8
|
32.3
|
1.0
|
CB
|
F:TYR200
|
5.0
|
31.6
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 6ub9
Go back to
Chlorine Binding Sites List in 6ub9
Chlorine binding site 4 out
of 4 in the Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form
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 Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Cl503
b:42.7
occ:1.00
|
CL1
|
H:H9V503
|
0.0
|
42.7
|
1.0
|
C10
|
H:H9V503
|
1.7
|
41.7
|
1.0
|
C11
|
H:H9V503
|
2.7
|
41.2
|
1.0
|
C9
|
H:H9V503
|
2.7
|
40.6
|
1.0
|
CD2
|
H:PHE211
|
3.4
|
23.9
|
1.0
|
CE2
|
H:PHE211
|
3.4
|
22.6
|
1.0
|
CB
|
H:PHE202
|
3.4
|
28.1
|
1.0
|
CG
|
H:PHE211
|
3.6
|
21.6
|
1.0
|
CG
|
H:PHE202
|
3.6
|
27.1
|
1.0
|
CZ
|
H:PHE211
|
3.6
|
22.4
|
1.0
|
CD1
|
H:PHE211
|
3.7
|
23.5
|
1.0
|
CE1
|
H:PHE211
|
3.7
|
23.6
|
1.0
|
C12
|
H:H9V503
|
4.0
|
42.3
|
1.0
|
C8
|
H:H9V503
|
4.0
|
40.1
|
1.0
|
CD1
|
H:PHE202
|
4.0
|
27.3
|
1.0
|
CD2
|
H:TYR200
|
4.0
|
29.8
|
1.0
|
CD2
|
H:PHE202
|
4.0
|
24.1
|
1.0
|
CE2
|
H:TYR200
|
4.2
|
30.8
|
1.0
|
CD
|
H:PRO208
|
4.2
|
23.2
|
1.0
|
CB
|
H:PHE211
|
4.4
|
21.3
|
1.0
|
CG
|
H:TYR200
|
4.4
|
28.1
|
1.0
|
C7
|
H:H9V503
|
4.5
|
40.9
|
1.0
|
CZ3
|
H:TRP191
|
4.7
|
26.2
|
1.0
|
CZ
|
H:TYR200
|
4.7
|
31.5
|
1.0
|
CA
|
H:PHE202
|
4.7
|
29.2
|
1.0
|
CG
|
H:PRO208
|
4.8
|
23.6
|
1.0
|
CE1
|
H:PHE202
|
4.8
|
27.6
|
1.0
|
CE2
|
H:PHE202
|
4.8
|
25.4
|
1.0
|
CD1
|
H:TYR200
|
4.9
|
29.0
|
1.0
|
F1
|
H:H9V503
|
5.0
|
45.6
|
1.0
|
O
|
H:TYR200
|
5.0
|
26.7
|
1.0
|
CB
|
H:TYR200
|
5.0
|
27.8
|
1.0
|
CA
|
H:GLY207
|
5.0
|
26.9
|
1.0
|
F2
|
H:H9V503
|
5.0
|
40.5
|
1.0
|
|
Reference:
C.Chang,
K.Michalska,
N.I.Maltseva,
R.Jedrzejczak,
P.Mccarren,
P.P.Nag,
A.Joachimiak,
K.Satchell,
Center For Structural Genomics Of Infectious Diseases(Csgid).
Crystal Structure of Tryptophan Synthase From M. Tuberculosis - Aminoacrylate- and BRD6309-Bound Form To Be Published.
Page generated: Mon Jul 29 15:48:38 2024
|