Chlorine in PDB 8oqu: Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92

Enzymatic activity of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92

All present enzymatic activity of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92:
1.1.1.35;

Protein crystallography data

The structure of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92, PDB code: 8oqu was solved by S.Dalwani, R.K.Wierenga, R.Venkatesan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 116.86 / 2.89
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 249.462, 134.892, 119.476, 90, 110.47, 90
R / Rfree (%) 18 / 21.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92 (pdb code 8oqu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92, PDB code: 8oqu:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 8oqu

Go back to Chlorine Binding Sites List in 8oqu
Chlorine binding site 1 out of 6 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl808

b:131.4
occ:1.00
 CL A:VXN808 0.0 131.4 1.0
C2 A:VXN808 1.7 97.4 1.0
C3 A:VXN808 2.7 95.4 1.0
C1 A:VXN808 2.7 91.0 1.0
O A:MET30 3.3 83.6 1.0
N A:ASP69 3.3 91.6 1.0
CE A:MET73 3.7 86.1 1.0
CB A:ASP69 3.8 79.6 1.0
O A:ASP69 3.9 97.9 1.0
CA A:ASP69 4.0 83.0 1.0
C A:VXN808 4.0 91.4 1.0
C4 A:VXN808 4.0 95.8 1.0
C A:GLY68 4.2 84.5 1.0
CA A:GLY68 4.2 92.1 1.0
C A:ASP69 4.3 88.4 1.0
C A:MET30 4.4 74.0 1.0
C5 A:VXN808 4.5 88.5 1.0
CL A:VXN810 4.8 140.5 1.0
SD A:MET73 4.9 108.8 1.0
CA A:ASN31 4.9 60.5 1.0
CG A:MET30 4.9 59.5 1.0

Chlorine binding site 2 out of 6 in 8oqu

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Chlorine binding site 2 out of 6 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl809

b:99.1
occ:1.00
 CL A:VXN809 0.0 99.1 1.0
C2 A:VXN809 1.7 92.4 1.0
C1 A:VXN809 2.7 90.7 1.0
C3 A:VXN809 2.7 98.3 1.0
CE A:MET73 3.4 86.1 1.0
C1 A:VXN808 3.8 91.0 1.0
CG2 A:THR87 4.0 54.1 1.0
C A:VXN809 4.0 86.3 1.0
C4 A:VXN809 4.0 100.0 1.0
C A:VXN808 4.0 91.4 1.0
CB A:THR87 4.1 57.6 1.0
CG1 A:VAL84 4.2 56.0 1.0
CA A:VAL84 4.3 61.5 1.0
CG2 A:VAL84 4.3 64.2 1.0
OG1 A:THR87 4.4 60.7 1.0
C5 A:VXN809 4.5 82.7 1.0
CB A:VAL84 4.5 59.2 1.0
C2 A:VXN808 4.5 97.4 1.0
O A:VAL84 4.6 54.5 1.0
C5 A:VXN808 4.9 88.5 1.0
CE2 A:PHE287 4.9 49.1 1.0
C A:VAL84 5.0 53.5 1.0
SD A:MET73 5.0 108.8 1.0

Chlorine binding site 3 out of 6 in 8oqu

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Chlorine binding site 3 out of 6 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl810

b:140.5
occ:1.00
 CL A:VXN810 0.0 140.5 1.0
C2 A:VXN810 1.7 130.7 1.0
C1 A:VXN810 2.7 90.6 1.0
C3 A:VXN810 2.7 128.8 1.0
CG2 A:VAL70 3.6 89.0 1.0
C A:GLY68 3.8 84.5 1.0
CA A:GLY68 3.8 92.1 1.0
N A:GLY68 3.9 83.0 1.0
N A:ASP69 4.0 91.6 1.0
C A:VXN810 4.0 69.8 1.0
C4 A:VXN810 4.0 116.1 1.0
SD A:MET73 4.0 108.8 1.0
N A:VAL70 4.0 68.8 1.0
CA A:VAL70 4.0 76.5 1.0
C A:ASP69 4.0 88.4 1.0
O A:ASP69 4.1 97.9 1.0
O A:GLY68 4.2 59.1 1.0
CB A:VAL70 4.4 77.9 1.0
C5 A:VXN810 4.5 101.6 1.0
CB A:MET73 4.5 79.5 1.0
CD1 A:LEU146 4.6 48.4 1.0
CA A:ASP69 4.7 83.0 1.0
CE A:MET73 4.7 86.1 1.0
CL A:VXN808 4.8 131.4 1.0
CG A:MET73 4.8 93.0 1.0
CG1 A:VAL70 4.9 66.8 1.0

Chlorine binding site 4 out of 6 in 8oqu

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Chlorine binding site 4 out of 6 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl807

b:97.1
occ:1.00
 CL B:VXN807 0.0 97.1 1.0
C2 B:VXN807 1.7 79.2 1.0
C1 B:VXN807 2.7 75.3 1.0
C3 B:VXN807 2.7 81.2 1.0
C3 B:VXN808 3.5 79.0 1.0
CG1 B:VAL84 3.9 41.6 1.0
C B:VXN807 4.0 64.8 1.0
C4 B:VXN807 4.0 79.0 1.0
C4 B:VXN808 4.0 103.3 1.0
CG B:MET73 4.0 74.5 1.0
O1 B:GOL806 4.1 106.1 1.0
CE2 B:PHE287 4.2 48.5 1.0
SD B:MET73 4.2 96.1 1.0
CG2 B:THR87 4.2 65.2 1.0
CB B:THR87 4.4 57.6 1.0
C2 B:VXN808 4.4 88.1 1.0
CA B:VAL84 4.5 54.9 1.0
C5 B:VXN807 4.5 64.4 1.0
CG2 B:VAL84 4.5 54.6 1.0
CB B:VAL84 4.5 56.8 1.0
O B:VAL84 4.6 57.5 1.0
CE B:MET73 4.6 96.5 1.0
CL B:VXN808 4.7 139.9 1.0
CG1 B:VAL88 4.8 63.8 1.0
CZ B:PHE287 4.8 61.6 1.0
OG1 B:THR87 4.9 60.3 1.0

Chlorine binding site 5 out of 6 in 8oqu

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Chlorine binding site 5 out of 6 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl808

b:139.9
occ:1.00
 CL B:VXN808 0.0 139.9 1.0
C2 B:VXN808 1.7 88.1 1.0
C1 B:VXN808 2.7 104.5 1.0
C3 B:VXN808 2.7 79.0 1.0
O B:MET30 3.0 65.4 1.0
CE B:MET73 3.3 96.5 1.0
N B:ASP69 3.7 93.3 1.0
C B:VXN808 4.0 101.5 1.0
C4 B:VXN808 4.0 103.3 1.0
CB B:ASP69 4.0 65.2 1.0
O1 B:GOL806 4.1 106.1 1.0
C B:MET30 4.1 63.5 1.0
CA B:ASP69 4.3 74.3 1.0
O B:ASP69 4.5 89.6 1.0
C5 B:VXN808 4.5 103.0 1.0
CA B:ASN31 4.6 61.7 1.0
C1 B:GOL806 4.6 64.4 1.0
CA B:GLY68 4.6 95.3 1.0
C B:GLY68 4.6 90.8 1.0
SD B:MET73 4.7 96.1 1.0
CL B:VXN807 4.7 97.1 1.0
C B:ASP69 4.7 89.8 1.0
N B:ASN31 4.8 66.9 1.0
CG B:MET30 5.0 52.6 1.0

Chlorine binding site 6 out of 6 in 8oqu

Go back to Chlorine Binding Sites List in 8oqu
Chlorine binding site 6 out of 6 in the Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Structure of Mycobacterium Tuberculosis Beta-Oxidation Trifunctional Enzyme in Complex with Fragment-M-92 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl809

b:182.3
occ:1.00
 CL B:VXN809 0.0 182.3 1.0
C2 B:VXN809 1.7 151.7 1.0
C1 B:VXN809 2.7 136.3 1.0
C3 B:VXN809 2.7 121.9 1.0
CE B:MET73 3.3 96.5 1.0
CG2 B:VAL70 3.4 90.4 1.0
CA B:GLY68 3.5 95.3 1.0
C B:GLY68 3.6 90.8 1.0
N B:GLY68 3.6 82.0 1.0
O B:GLY68 4.0 75.0 1.0
N B:VAL70 4.0 80.7 1.0
C B:VXN809 4.0 118.8 1.0
C4 B:VXN809 4.0 95.7 1.0
N B:ASP69 4.0 93.3 1.0
CA B:VAL70 4.1 70.7 1.0
SD B:MET73 4.2 96.1 1.0
CB B:VAL70 4.2 75.4 1.0
C B:ASP69 4.3 89.8 1.0
O2 B:GOL806 4.4 101.9 1.0
C5 B:VXN809 4.5 108.4 1.0
O B:ASP69 4.6 89.6 1.0
C B:GLY67 4.7 79.5 1.0
CG1 B:VAL70 4.7 59.4 1.0
CD1 B:LEU146 4.8 47.4 1.0
CA B:ASP69 4.8 74.3 1.0

Reference:

S.Dalwani, A.Metz, F.U.Huschmann, M.S.Weiss, R.K.Wierenga, R.Venkatesan. Crystallographic Fragment Binding Studies of the Mycobacterium Tuberculosis Trifunctional Enzyme Suggest Binding Pockets For the Tails of the Acyl-Coa Substrates at Its Active Sites and A Potential Substrate Channeling Path Between Them Biorxiv 2024.
ISSN: ISSN 2692-8205
DOI: 10.1101/2024.01.11.575214
Page generated: Tue Jul 30 11:15:57 2024

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