Manganese in PDB 5jbi: Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese

All present enzymatic activity of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese:
1.1.1.267;

The structure of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese, PDB code: 5jbi was solved by S.Sooriyaarachchi, T.Bergfors, T.A.Jones, S.L.Mowbray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.657, 56.397, 85.919, 103.60, 102.96, 100.46
R / Rfree (%)	17.9 / 21

The binding sites of Manganese atom in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese (pdb code 5jbi). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese, PDB code: 5jbi:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:19.0 occ:1.00 OE1 A:GLU233 2.1 18.0 1.0 OE2 A:GLU315 2.1 17.1 1.0 OD1 A:ASP231 2.1 21.0 1.0 O12 A:6J8501 2.2 20.1 1.0 O10 A:6J8501 2.2 23.2 1.0 OE2 A:GLU233 2.7 19.9 1.0 CD A:GLU233 2.7 18.0 1.0 C4 A:6J8501 2.8 23.4 1.0 N9 A:6J8501 2.9 23.5 1.0 CD A:GLU315 3.0 17.6 1.0 CG A:ASP231 3.1 20.6 1.0 OE1 A:GLU315 3.5 19.0 1.0 NZ A:LYS205 3.5 28.9 1.0 OD2 A:ASP231 3.5 20.9 1.0 OG A:SER232 3.9 19.1 1.0 O A:HOH635 3.9 38.4 1.0 N A:SER232 4.1 17.8 1.0 ND2 A:ASN311 4.2 17.6 1.0 CG A:GLU233 4.2 17.0 1.0 CG A:GLU315 4.3 15.8 1.0 C3 A:6J8501 4.3 23.9 1.0 C11 A:6J8501 4.3 23.7 1.0 CB A:ASP231 4.4 19.2 1.0 N A:GLU233 4.5 15.3 1.0 NZ A:LYS312 4.6 17.0 1.0 C2 A:6J8501 4.7 25.0 1.0 C A:ASP231 4.7 18.7 1.0 CA A:ASP231 4.7 18.4 1.0 CE A:LYS205 4.8 28.9 1.0 CB A:GLU233 4.9 15.8 1.0 CB A:SER232 4.9 18.6 1.0 CA A:SER232 4.9 17.2 1.0

Manganese binding site 2 out of 2 in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC52 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:17.9 occ:1.00 OE1 B:GLU233 2.1 17.1 1.0 O12 B:6J8501 2.1 20.7 1.0 OE2 B:GLU315 2.1 16.5 1.0 OD1 B:ASP231 2.1 19.1 1.0 O10 B:6J8501 2.3 23.0 1.0 OE2 B:GLU233 2.7 17.1 1.0 CD B:GLU233 2.7 15.8 1.0 C4 B:6J8501 2.8 22.9 1.0 N9 B:6J8501 2.9 23.0 1.0 CD B:GLU315 3.0 16.4 1.0 CG B:ASP231 3.1 19.4 1.0 OE1 B:GLU315 3.4 18.1 1.0 OD2 B:ASP231 3.5 20.2 1.0 NZ B:LYS205 3.6 28.3 1.0 OG B:SER232 4.0 18.5 1.0 N B:SER232 4.1 16.8 1.0 O B:HOH682 4.1 43.7 1.0 O B:HOH615 4.2 39.6 1.0 ND2 B:ASN311 4.2 19.2 1.0 CG B:GLU233 4.2 15.2 1.0 C3 B:6J8501 4.2 24.4 1.0 CG B:GLU315 4.3 15.0 1.0 C11 B:6J8501 4.3 23.7 1.0 CB B:ASP231 4.4 18.5 1.0 N B:GLU233 4.5 14.2 1.0 C2 B:6J8501 4.6 25.6 1.0 NZ B:LYS312 4.6 19.4 1.0 C B:ASP231 4.6 16.9 1.0 CA B:ASP231 4.7 17.0 1.0 CB B:GLU233 4.8 14.5 1.0 CB B:SER232 4.9 17.4 1.0 CA B:SER232 4.9 16.0 1.0 CE B:LYS205 4.9 28.3 1.0

S.Sooriyaarachchi, R.Chofor, M.D.Risseeuw, T.Bergfors, J.Pouyez, C.S.Dowd, L.Maes, J.Wouters, T.A.Jones, S.Van Calenbergh, S.L.Mowbray. Targeting An Aromatic Hotspot in Plasmodium Falciparum 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase with Beta-Arylpropyl Analogues of Fosmidomycin. Chemmedchem V. 11 2024 2016.
ISSN: ESSN 1860-7187
PubMed: 27487410
DOI: 10.1002/CMDC.201600249