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Chlorine in PDB 5mut: Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds

Enzymatic activity of Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds

All present enzymatic activity of Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds:
1.3.5.2;

Protein crystallography data

The structure of Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds, PDB code: 5mut was solved by P.Goyal, M.Andersson, A.C.Moritzer, S.Sainas, A.C.Pippione, D.Boschi, S.Al-Kadaraghi, M.Lolli, R.Friemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.81 / 1.75
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.080, 91.080, 122.522, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 19.8

Other elements in 5mut:

The structure of Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds (pdb code 5mut). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds, PDB code: 5mut:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 5mut

Go back to Chlorine Binding Sites List in 5mut
Chlorine binding site 1 out of 3 in the Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds


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 Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:12.9
occ:1.00
 N A:ARG136 3.3 6.9 1.0
O A:HOH694 3.6 30.6 1.0
O A:HOH747 3.6 27.1 1.0
O A:HOH551 3.7 18.3 1.0
CD1 A:LEU297 3.7 9.6 1.0
CD A:PRO52 3.8 12.5 1.0
CA A:PHE135 3.9 9.9 1.0
CG A:PRO52 3.9 10.4 1.0
C A:PHE135 4.1 8.3 1.0
CB A:ARG136 4.2 7.6 1.0
CG A:ARG136 4.2 8.0 1.0
CA A:ARG136 4.2 7.4 1.0
O A:ARG136 4.4 6.3 1.0
CB A:PHE135 4.5 7.3 1.0
O A:VAL134 4.6 8.3 1.0
CD1 A:PHE135 4.7 5.9 1.0
C A:ARG136 4.8 6.8 1.0
N A:PHE135 5.0 5.3 1.0

Chlorine binding site 2 out of 3 in 5mut

Go back to Chlorine Binding Sites List in 5mut
Chlorine binding site 2 out of 3 in the Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds


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 Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl407

b:8.1
occ:1.00
 OG A:SER299 3.1 7.2 1.0
NE A:ARG298 3.2 7.9 1.0
O A:HOH752 3.3 23.8 1.0
NH2 A:ARG298 3.4 8.0 1.0
CZ A:ARG298 3.7 10.7 1.0
CB A:SER299 4.1 4.5 1.0
CG A:ARG298 4.3 5.3 1.0
CD A:ARG298 4.3 5.0 1.0
O A:HOH576 4.8 20.2 1.0
O A:HOH779 4.9 29.9 1.0

Chlorine binding site 3 out of 3 in 5mut

Go back to Chlorine Binding Sites List in 5mut
Chlorine binding site 3 out of 3 in the Crystal Structure of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds


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 Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl408

b:15.7
occ:1.00
 O A:HOH756 3.0 24.8 1.0
O A:HOH672 3.0 18.4 1.0
N A:GLY302 3.2 6.1 1.0
O A:GLY302 3.7 7.3 1.0
CA A:THR301 3.8 6.5 1.0
CG2 A:THR301 3.8 12.5 1.0
C A:THR301 4.0 5.2 1.0
NH2 A:ARG289 4.1 4.2 1.0
CA A:GLY302 4.2 5.5 1.0
CB A:THR301 4.2 6.2 1.0
C A:GLY302 4.3 6.1 1.0
CB A:VAL287 4.4 9.9 1.0
OG1 A:THR301 4.4 8.9 1.0
O A:VAL287 4.5 6.4 1.0
CG1 A:VAL287 4.5 10.6 1.0
O A:HOH785 4.7 33.0 1.0
CZ A:ARG289 4.8 4.1 1.0
CA A:VAL287 4.8 4.7 1.0
O A:GLU300 4.9 5.3 1.0
NH1 A:ARG289 5.0 5.8 1.0

Reference:

S.Sainas, A.C.Pippione, M.Giorgis, E.Lupino, P.Goyal, C.Ramondetti, B.Buccinna, M.Piccinini, R.C.Braga, C.H.Andrade, M.Andersson, A.C.Moritzer, R.Friemann, S.Mensa, S.Al-Kadaraghi, D.Boschi, M.L.Lolli. Design, Synthesis, Biological Evaluation and X-Ray Structural Studies of Potent Human Dihydroorotate Dehydrogenase Inhibitors Based on Hydroxylated Azole Scaffolds. Eur J Med Chem V. 129 287 2017.
ISSN: ISSN 1768-3254
PubMed: 28235702
DOI: 10.1016/J.EJMECH.2017.02.017
Page generated: Fri Jul 26 12:56:21 2024

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