Manganese in PDB 5jmw: Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC50 and Manganese

All present enzymatic activity of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC50 and Manganese:
1.1.1.267;

The structure of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC50 and Manganese, PDB code: 5jmw 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)	28.00 / 1.55
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.430, 56.193, 86.046, 103.57, 103.07, 100.40
R / Rfree (%)	18 / 20.2

The binding sites of Manganese atom in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC50 and Manganese (pdb code 5jmw). 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, LC50 and Manganese, PDB code: 5jmw:
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, LC50 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, LC50 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:11.3 occ:1.00 OE1 A:GLU233 2.1 11.1 1.0 OE2 A:GLU315 2.1 10.0 1.0 OD1 A:ASP231 2.1 11.3 1.0 O10 A:L50501 2.2 13.1 1.0 O12 A:L50501 2.2 13.5 1.0 CD A:GLU233 2.8 10.6 1.0 OE2 A:GLU233 2.9 11.2 1.0 C4 A:L50501 2.9 14.8 1.0 N9 A:L50501 2.9 14.2 1.0 CD A:GLU315 3.1 9.2 1.0 CG A:ASP231 3.1 11.1 1.0 OD2 A:ASP231 3.5 11.1 1.0 OE1 A:GLU315 3.5 9.7 1.0 NZ A:LYS205 3.5 17.1 1.0 O A:HOH657 3.7 26.0 1.0 OG A:SER232 3.9 11.1 1.0 N A:SER232 4.0 10.3 1.0 O A:HOH604 4.0 23.2 1.0 ND2 A:ASN311 4.2 11.6 1.0 CG A:GLU315 4.3 8.9 1.0 CG A:GLU233 4.3 10.2 1.0 C3 A:L50501 4.3 15.7 1.0 C11 A:L50501 4.3 14.2 1.0 CB A:ASP231 4.4 10.9 1.0 N A:GLU233 4.4 9.7 1.0 C A:ASP231 4.6 10.6 1.0 NZ A:LYS312 4.7 12.6 1.0 CA A:ASP231 4.7 10.7 1.0 C2 A:L50501 4.7 16.8 1.0 CB A:SER232 4.8 10.5 1.0 CE A:LYS205 4.8 17.6 1.0 CA A:SER232 4.8 10.3 1.0 CB A:GLU233 4.9 9.9 1.0

Manganese binding site 2 out of 2 in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC50 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, LC50 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:10.2 occ:1.00 OE1 B:GLU233 2.1 10.1 1.0 OE2 B:GLU315 2.1 9.3 1.0 OD1 B:ASP231 2.1 10.2 1.0 O10 B:L50501 2.2 11.9 1.0 O12 B:L50501 2.2 12.3 1.0 CD B:GLU233 2.8 9.7 1.0 OE2 B:GLU233 2.9 10.2 1.0 C4 B:L50501 2.9 13.6 1.0 N9 B:L50501 2.9 13.0 1.0 CD B:GLU315 3.1 8.9 1.0 CG B:ASP231 3.1 10.1 1.0 OE1 B:GLU315 3.5 9.4 1.0 NZ B:LYS205 3.5 16.3 1.0 OD2 B:ASP231 3.5 10.3 1.0 OG B:SER232 3.8 10.2 1.0 O B:HOH659 3.8 29.6 1.0 N B:SER232 4.0 9.5 1.0 O B:HOH603 4.0 26.8 1.0 ND2 B:ASN311 4.2 10.4 1.0 CG B:GLU315 4.3 8.7 1.0 C3 B:L50501 4.3 14.5 1.0 CG B:GLU233 4.3 9.5 1.0 C11 B:L50501 4.3 13.2 1.0 CB B:ASP231 4.4 9.8 1.0 N B:GLU233 4.4 8.9 1.0 C B:ASP231 4.5 9.5 1.0 NZ B:LYS312 4.6 11.6 1.0 C2 B:L50501 4.7 15.9 1.0 CA B:ASP231 4.7 9.7 1.0 CB B:SER232 4.7 9.5 1.0 CA B:SER232 4.8 9.4 1.0 CE B:LYS205 4.8 16.6 1.0 CB B:GLU233 4.8 9.1 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