Chlorine in PDB 8a1o: Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8
Protein crystallography data
The structure of Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8, PDB code: 8a1o
was solved by
M.De Munnik,
P.A.Lang,
J.Brem,
C.J.Schofield,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.50 /
1.95
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
76.87,
93,
61.4,
90,
90,
90
|
R / Rfree (%)
|
18.8 /
22.5
|
Other elements in 8a1o:
The structure of Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8
(pdb code 8a1o). 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 Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8, PDB code: 8a1o:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 8a1o
Go back to
Chlorine Binding Sites List in 8a1o
Chlorine binding site 1 out
of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8
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 Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1004
b:54.5
occ:1.00
|
CL16
|
A:KTI1004
|
0.0
|
54.5
|
1.0
|
C15
|
A:KTI1004
|
1.8
|
54.7
|
1.0
|
C14
|
A:KTI1004
|
2.7
|
54.5
|
1.0
|
C17
|
A:KTI1004
|
2.7
|
54.6
|
1.0
|
C13
|
A:KTI1004
|
3.0
|
52.3
|
1.0
|
C10
|
A:KTI1004
|
3.3
|
46.3
|
1.0
|
NE2
|
A:HIS336
|
3.4
|
37.9
|
1.0
|
CG2
|
A:VAL322
|
3.5
|
41.4
|
1.0
|
CD2
|
A:HIS336
|
3.5
|
37.2
|
1.0
|
SD
|
A:MET303
|
3.5
|
46.8
|
1.0
|
CL22
|
A:KTI1004
|
3.6
|
46.0
|
1.0
|
CE
|
A:MET303
|
3.6
|
46.0
|
1.0
|
S11
|
A:KTI1004
|
3.8
|
49.3
|
1.0
|
C03
|
A:KTI1004
|
3.8
|
43.0
|
1.0
|
C20
|
A:KTI1004
|
4.0
|
55.2
|
1.0
|
C18
|
A:KTI1004
|
4.0
|
55.5
|
1.0
|
CG1
|
A:VAL322
|
4.0
|
40.6
|
1.0
|
N23
|
A:KTI1004
|
4.1
|
43.2
|
1.0
|
CE1
|
A:HIS336
|
4.1
|
39.1
|
1.0
|
CB
|
A:VAL322
|
4.3
|
40.3
|
1.0
|
CG
|
A:HIS336
|
4.3
|
36.5
|
1.0
|
SG
|
A:CYS354
|
4.5
|
38.2
|
1.0
|
C19
|
A:KTI1004
|
4.5
|
56.1
|
1.0
|
C02
|
A:KTI1004
|
4.5
|
44.3
|
1.0
|
ND1
|
A:HIS336
|
4.5
|
38.5
|
1.0
|
O12
|
A:KTI1004
|
4.7
|
50.1
|
1.0
|
CG
|
A:MET303
|
4.8
|
45.7
|
1.0
|
O21
|
A:KTI1004
|
4.8
|
50.6
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 8a1o
Go back to
Chlorine Binding Sites List in 8a1o
Chlorine binding site 2 out
of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8
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 Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1004
b:46.0
occ:1.00
|
CL22
|
A:KTI1004
|
0.0
|
46.0
|
1.0
|
C10
|
A:KTI1004
|
1.7
|
46.3
|
1.0
|
C03
|
A:KTI1004
|
2.7
|
43.0
|
1.0
|
S11
|
A:KTI1004
|
2.9
|
49.3
|
1.0
|
SG
|
A:CYS354
|
3.0
|
38.2
|
1.0
|
O
|
A:GLY332
|
3.0
|
38.8
|
1.0
|
O21
|
A:KTI1004
|
3.1
|
50.6
|
1.0
|
CD2
|
A:PHE334
|
3.4
|
33.2
|
1.0
|
CL16
|
A:KTI1004
|
3.6
|
54.5
|
1.0
|
C13
|
A:KTI1004
|
3.7
|
52.3
|
1.0
|
SD
|
A:MET303
|
4.0
|
46.8
|
1.0
|
CL
|
A:CL1007
|
4.1
|
86.3
|
1.0
|
CE2
|
A:PHE334
|
4.1
|
34.7
|
1.0
|
C02
|
A:KTI1004
|
4.1
|
44.3
|
1.0
|
O12
|
A:KTI1004
|
4.1
|
50.1
|
1.0
|
CG
|
A:PHE334
|
4.2
|
32.1
|
1.0
|
C
|
A:GLY332
|
4.2
|
36.5
|
1.0
|
CB
|
A:PHE334
|
4.3
|
31.1
|
1.0
|
CE
|
A:MET303
|
4.4
|
46.0
|
1.0
|
C15
|
A:KTI1004
|
4.6
|
54.7
|
1.0
|
C14
|
A:KTI1004
|
4.6
|
54.5
|
1.0
|
N
|
A:PHE334
|
4.6
|
32.4
|
1.0
|
CB
|
A:CYS354
|
4.8
|
37.1
|
1.0
|
CL
|
A:CL1006
|
4.8
|
72.1
|
1.0
|
N23
|
A:KTI1004
|
4.8
|
43.2
|
1.0
|
O01
|
A:KTI1004
|
4.9
|
46.3
|
1.0
|
CA
|
A:GLY332
|
4.9
|
37.9
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 8a1o
Go back to
Chlorine Binding Sites List in 8a1o
Chlorine binding site 3 out
of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8
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 Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1006
b:72.1
occ:1.00
|
O
|
A:GLY332
|
3.3
|
38.8
|
1.0
|
C
|
A:GLY332
|
3.6
|
36.5
|
1.0
|
O
|
A:HIS352
|
3.9
|
48.4
|
1.0
|
CA
|
A:GLY332
|
4.1
|
37.9
|
1.0
|
N
|
A:VAL333
|
4.2
|
33.6
|
1.0
|
O
|
A:SER331
|
4.2
|
36.6
|
1.0
|
C
|
A:HIS352
|
4.5
|
46.8
|
1.0
|
CA
|
A:VAL333
|
4.5
|
33.5
|
1.0
|
CA
|
A:GLY353
|
4.5
|
40.8
|
1.0
|
CG2
|
A:VAL333
|
4.5
|
35.9
|
1.0
|
O21
|
A:KTI1004
|
4.6
|
50.6
|
1.0
|
C10
|
A:KTI1004
|
4.7
|
46.3
|
1.0
|
N
|
A:GLY353
|
4.7
|
43.8
|
1.0
|
C
|
A:GLY353
|
4.7
|
38.2
|
1.0
|
N
|
A:CYS354
|
4.8
|
36.4
|
1.0
|
N
|
A:GLY332
|
4.8
|
35.7
|
1.0
|
C
|
A:SER331
|
4.8
|
36.7
|
1.0
|
CL22
|
A:KTI1004
|
4.8
|
46.0
|
1.0
|
C03
|
A:KTI1004
|
4.8
|
43.0
|
1.0
|
CB
|
A:HIS352
|
5.0
|
51.0
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 8a1o
Go back to
Chlorine Binding Sites List in 8a1o
Chlorine binding site 4 out
of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8
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 Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1007
b:86.3
occ:1.00
|
O
|
A:HOH1480
|
3.7
|
80.3
|
1.0
|
O
|
A:HOH1255
|
3.7
|
48.4
|
1.0
|
O
|
A:HOH1483
|
3.8
|
47.4
|
1.0
|
CE2
|
A:PHE334
|
3.9
|
34.7
|
1.0
|
CL22
|
A:KTI1004
|
4.1
|
46.0
|
1.0
|
SD
|
A:MET303
|
4.1
|
46.8
|
1.0
|
CA
|
A:GLY332
|
4.2
|
37.9
|
1.0
|
O
|
A:HOH1438
|
4.3
|
63.4
|
1.0
|
O
|
A:GLY332
|
4.5
|
38.8
|
1.0
|
O21
|
A:KTI1004
|
4.5
|
50.6
|
1.0
|
OH
|
A:TYR318
|
4.6
|
46.8
|
1.0
|
CD2
|
A:PHE334
|
4.6
|
33.2
|
1.0
|
CZ
|
A:PHE334
|
4.7
|
34.5
|
1.0
|
C
|
A:GLY332
|
4.8
|
36.5
|
1.0
|
OH
|
A:TYR308
|
4.9
|
66.4
|
1.0
|
CE2
|
A:TYR308
|
4.9
|
65.3
|
1.0
|
|
Reference:
M.De Munnik,
P.A.Lang,
J.Brem,
C.J.Schofield.
Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Acrylamide Analogue 8 To Be Published.
Page generated: Wed Jul 26 15:21:15 2023
|