Manganese in PDB 5jo0: Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC56 and Manganese

All present enzymatic activity of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC56 and Manganese:
1.1.1.267;

The structure of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC56 and Manganese, PDB code: 5jo0 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 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.755, 55.951, 85.619, 103.44, 103.03, 100.49
R / Rfree (%)	17.6 / 20.6

The binding sites of Manganese atom in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC56 and Manganese (pdb code 5jo0). 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, LC56 and Manganese, PDB code: 5jo0:
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, LC56 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, LC56 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:25.4 occ:1.00 OE1 A:GLU233 2.1 25.1 1.0 OE2 A:GLU315 2.1 22.4 1.0 OD1 A:ASP231 2.1 26.8 1.0 O10 A:L56501 2.2 28.6 1.0 O12 A:L56501 2.2 28.0 1.0 OE2 A:GLU233 2.6 24.4 1.0 CD A:GLU233 2.7 23.3 1.0 C4 A:L56501 2.8 30.4 1.0 N9 A:L56501 2.9 30.6 1.0 CD A:GLU315 3.0 21.9 1.0 CG A:ASP231 3.1 28.1 1.0 OD2 A:ASP231 3.5 27.9 1.0 OE1 A:GLU315 3.5 23.0 1.0 NZ A:LYS205 3.5 35.0 1.0 O A:HOH637 3.7 44.0 1.0 OG A:SER232 3.8 26.3 1.0 O A:HOH606 4.1 42.9 1.0 CG A:GLU233 4.1 21.9 1.0 N A:SER232 4.2 22.1 1.0 CG A:GLU315 4.2 19.5 1.0 ND2 A:ASN311 4.2 23.0 1.0 C3 A:L56501 4.2 30.8 1.0 C11 A:L56501 4.3 31.1 1.0 CB A:ASP231 4.3 25.9 1.0 N A:GLU233 4.4 18.8 1.0 NZ A:LYS312 4.5 22.5 1.0 C2 A:L56501 4.6 31.7 1.0 C A:ASP231 4.7 24.9 1.0 CA A:ASP231 4.7 24.7 1.0 CB A:GLU233 4.8 20.1 1.0 CB A:SER232 4.8 23.3 1.0 CE A:LYS205 4.9 36.3 1.0 CA A:SER232 4.9 21.4 1.0

Manganese binding site 2 out of 2 in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC56 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, LC56 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:21.8 occ:1.00 O12 B:L56501 2.1 24.8 1.0 OE1 B:GLU233 2.1 20.3 1.0 OD1 B:ASP231 2.1 22.4 1.0 OE2 B:GLU315 2.1 20.5 1.0 O10 B:L56501 2.2 24.7 1.0 OE2 B:GLU233 2.7 21.2 1.0 CD B:GLU233 2.7 19.2 1.0 C4 B:L56501 2.8 26.6 1.0 N9 B:L56501 2.8 26.0 1.0 CD B:GLU315 3.0 20.6 1.0 CG B:ASP231 3.1 23.4 1.0 OE1 B:GLU315 3.4 23.6 1.0 NZ B:LYS205 3.5 30.2 1.0 OD2 B:ASP231 3.5 24.6 1.0 O B:HOH669 3.7 40.2 1.0 OG B:SER232 3.9 20.3 1.0 O B:HOH602 4.1 36.9 1.0 N B:SER232 4.1 19.8 1.0 ND2 B:ASN311 4.1 20.5 1.0 C3 B:L56501 4.2 26.4 1.0 CG B:GLU233 4.2 18.0 1.0 C11 B:L56501 4.2 27.9 1.0 CG B:GLU315 4.3 18.0 1.0 CB B:ASP231 4.4 21.2 1.0 N B:GLU233 4.5 15.6 1.0 C2 B:L56501 4.5 27.1 1.0 NZ B:LYS312 4.6 21.3 1.0 C B:ASP231 4.6 20.2 1.0 CA B:ASP231 4.7 20.4 1.0 CB B:GLU233 4.8 16.8 1.0 CE B:LYS205 4.8 30.5 1.0 CB B:SER232 4.9 19.8 1.0 CA B:SER232 4.9 18.1 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