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Chlorine in PDB 5g22: Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26)

Enzymatic activity of Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26)

All present enzymatic activity of Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26):
2.3.1.97;

Protein crystallography data

The structure of Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26), PDB code: 5g22 was solved by V.Goncalves, J.A.Brannigan, A.Laporte, A.S.Bell, S.M.Roberts, A.J.Wilkinson, R.J.Leatherbarrow, E.W.Tate, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 101.64 / 2.32
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.970, 123.360, 179.370, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 28.3

Other elements in 5g22:

The structure of Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26) also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26) (pdb code 5g22). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26), PDB code: 5g22:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 5g22

Go back to Chlorine Binding Sites List in 5g22
Chlorine binding site 1 out of 3 in the Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1413

b:26.9
occ:1.00
 O A:HOH2079 3.1 22.4 1.0
NH2 A:ARG358 3.2 20.8 1.0
N A:LEU248 3.3 21.1 1.0
CA A:THR247 3.6 20.4 1.0
O A:HOH2111 3.7 11.2 1.0
C A:THR247 3.9 21.2 1.0
O A:ASP246 4.0 21.0 1.0
CB A:LEU248 4.1 22.9 1.0
CZ A:ARG358 4.1 20.8 1.0
CG A:LEU248 4.1 23.0 1.0
NH1 A:ARG358 4.2 19.2 1.0
CG2 A:THR247 4.2 18.3 1.0
CD1 A:LEU248 4.3 23.8 1.0
CA A:LEU248 4.3 23.4 1.0
CB A:THR247 4.4 18.9 1.0
N A:THR247 4.5 21.4 1.0
C A:ASP246 4.7 22.2 1.0
OG1 A:THR247 4.7 18.4 1.0
O A:LEU248 5.0 24.9 1.0

Chlorine binding site 2 out of 3 in 5g22

Go back to Chlorine Binding Sites List in 5g22
Chlorine binding site 2 out of 3 in the Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1412

b:29.1
occ:1.00
 NH2 B:ARG358 3.4 13.8 0.5
N B:LEU248 3.6 18.1 1.0
CD1 B:LEU248 3.8 23.1 1.0
CA B:THR247 3.8 16.4 1.0
NH2 B:ARG358 4.0 17.9 0.5
NH1 B:ARG358 4.1 17.4 0.5
O B:ASP246 4.1 18.1 1.0
CG B:LEU248 4.1 23.3 1.0
C B:THR247 4.2 16.9 1.0
CG2 B:THR247 4.3 15.2 1.0
CZ B:ARG358 4.3 14.2 0.5
NH1 B:ARG358 4.3 14.2 0.5
CB B:LEU248 4.3 21.8 1.0
CB B:THR247 4.4 16.1 1.0
OG1 B:THR247 4.4 16.7 1.0
CZ B:ARG358 4.5 17.8 0.5
CA B:LEU248 4.6 20.7 1.0
N B:THR247 4.8 16.8 1.0
C B:ASP246 4.8 18.1 1.0

Chlorine binding site 3 out of 3 in 5g22

Go back to Chlorine Binding Sites List in 5g22
Chlorine binding site 3 out of 3 in the Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Plasmodium Vivax N-Myristoyltransferase in Complex with A Quinoline Inhibitor (Compound 26) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1412

b:26.8
occ:1.00
 O C:HOH2027 3.4 13.8 1.0
NZ C:LYS180 3.6 18.6 1.0
CE1 C:TYR65 3.8 18.8 1.0
CD C:LYS180 4.0 16.8 1.0
CE C:LYS180 4.4 18.1 1.0
OH C:TYR65 4.5 20.1 1.0
CZ C:TYR65 4.6 19.6 1.0
CD1 C:TYR65 4.6 18.3 1.0

Reference:

V.Goncalves, J.A.Brannigan, A.Laporte, A.S.Bell, S.M.Roberts, A.J.Wilkinson, R.J.Leatherbarrow, E.W.Tate. Structure-Guided Optimization of Quinoline Inhibitors of Plasmodium N-Myristoyltransferase. Medchemcomm V. 8 191 2017.
ISSN: ISSN 2040-2503
PubMed: 28626547
DOI: 10.1039/C6MD00531D
Page generated: Fri Jul 26 08:18:33 2024

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