Manganese in PDB 5jc1: Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC55 and Manganese

All present enzymatic activity of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC55 and Manganese:
1.1.1.267;

The structure of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC55 and Manganese, PDB code: 5jc1 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 / 1.65
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.575, 56.459, 85.708, 103.84, 103.25, 100.15
R / Rfree (%)	17.9 / 20.4

The binding sites of Manganese atom in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC55 and Manganese (pdb code 5jc1). 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, LC55 and Manganese, PDB code: 5jc1:
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, LC55 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, LC55 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:12.8 occ:1.00 OE1 A:GLU233 2.1 12.7 1.0 OD1 A:ASP231 2.1 12.9 1.0 OE2 A:GLU315 2.1 11.1 1.0 O12 A:6JB501 2.2 14.8 1.0 O10 A:6JB501 2.2 15.2 1.0 CD A:GLU233 2.8 12.8 1.0 OE2 A:GLU233 2.8 13.7 1.0 C4 A:6JB501 2.9 16.1 1.0 N9 A:6JB501 2.9 16.3 1.0 CD A:GLU315 3.1 10.7 1.0 CG A:ASP231 3.1 12.3 1.0 OE1 A:GLU315 3.5 11.2 1.0 OD2 A:ASP231 3.5 12.2 1.0 NZ A:LYS205 3.5 19.6 1.0 OG A:SER232 3.8 13.1 1.0 O A:HOH690 3.9 31.3 1.0 N A:SER232 4.1 11.7 1.0 ND2 A:ASN311 4.2 11.8 1.0 CG A:GLU315 4.3 10.4 1.0 CG A:GLU233 4.3 12.2 1.0 C3 A:6JB501 4.3 16.2 1.0 C11 A:6JB501 4.3 16.3 1.0 CB A:ASP231 4.4 12.1 1.0 N A:GLU233 4.4 11.0 1.0 C A:ASP231 4.6 12.0 1.0 CA A:ASP231 4.7 11.9 1.0 C2 A:6JB501 4.7 16.9 1.0 NZ A:LYS312 4.7 11.8 1.0 CE A:LYS205 4.8 20.0 1.0 CB A:SER232 4.8 12.1 1.0 CB A:GLU233 4.9 11.5 1.0 CA A:SER232 4.9 11.7 1.0

Manganese binding site 2 out of 2 in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC55 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, LC55 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn503 b:12.1 occ:1.00 OE1 B:GLU233 2.1 12.0 1.0 OE2 B:GLU315 2.1 10.5 1.0 OD1 B:ASP231 2.1 12.8 1.0 O12 B:6JB502 2.2 13.3 1.0 O10 B:6JB502 2.2 13.8 1.0 CD B:GLU233 2.8 11.4 1.0 OE2 B:GLU233 2.8 11.9 1.0 C4 B:6JB502 2.9 14.7 1.0 N9 B:6JB502 2.9 14.6 1.0 CD B:GLU315 3.0 10.4 1.0 CG B:ASP231 3.1 12.7 1.0 OE1 B:GLU315 3.4 10.9 1.0 OD2 B:ASP231 3.5 13.2 1.0 NZ B:LYS205 3.6 20.3 1.0 OG B:SER232 3.9 11.8 1.0 N B:SER232 4.0 10.9 1.0 O B:HOH647 4.2 27.8 1.0 O B:HOH742 4.2 34.7 1.0 ND2 B:ASN311 4.2 12.1 1.0 CG B:GLU315 4.2 10.3 1.0 CG B:GLU233 4.3 10.9 1.0 C3 B:6JB502 4.3 15.1 1.0 C11 B:6JB502 4.3 14.8 1.0 CB B:ASP231 4.4 12.1 1.0 N B:GLU233 4.5 9.9 1.0 C B:ASP231 4.6 11.0 1.0 C2 B:6JB502 4.6 15.6 1.0 NZ B:LYS312 4.7 11.9 1.0 CA B:ASP231 4.7 11.5 1.0 CB B:SER232 4.8 11.0 1.0 CB B:GLU233 4.8 10.3 1.0 CA B:SER232 4.9 10.7 1.0 CE B:LYS205 4.9 20.5 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