Manganese in PDB 5jaz: Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC51 and Manganese

All present enzymatic activity of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC51 and Manganese:
1.1.1.267;

The structure of Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC51 and Manganese, PDB code: 5jaz 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 / 1.40
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.768, 56.543, 87.000, 103.66, 103.34, 100.18
R / Rfree (%)	18.5 / 20.7

The binding sites of Manganese atom in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC51 and Manganese (pdb code 5jaz). 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, LC51 and Manganese, PDB code: 5jaz:
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, LC51 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, LC51 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:8.2 occ:1.00 OE1 A:GLU233 2.1 8.6 1.0 OE2 A:GLU315 2.1 8.2 1.0 OD1 A:ASP231 2.1 9.1 1.0 O10 A:LC5501 2.2 9.9 1.0 O12 A:LC5501 2.2 9.4 1.0 CD A:GLU233 2.8 8.4 1.0 OE2 A:GLU233 2.8 9.4 1.0 C4 A:LC5501 2.9 10.3 1.0 N9 A:LC5501 2.9 10.0 1.0 CD A:GLU315 3.1 7.7 1.0 CG A:ASP231 3.1 8.9 1.0 OE1 A:GLU315 3.5 8.2 1.0 OD2 A:ASP231 3.5 9.0 1.0 NZ A:LYS205 3.6 13.2 1.0 O A:HOH700 3.6 20.2 1.0 OG A:SER232 3.8 7.8 1.0 N A:SER232 4.0 7.9 1.0 O A:HOH602 4.1 19.3 1.0 CG A:GLU233 4.3 8.0 1.0 C3 A:LC5501 4.3 10.5 1.0 CG A:GLU315 4.3 7.5 1.0 C11 A:LC5501 4.3 10.2 1.0 ND2 A:ASN311 4.3 7.9 1.0 CB A:ASP231 4.4 8.4 1.0 N A:GLU233 4.4 7.1 1.0 C A:ASP231 4.6 8.1 1.0 NZ A:LYS312 4.7 9.6 1.0 C2 A:LC5501 4.7 10.9 1.0 CA A:ASP231 4.7 8.3 1.0 CB A:SER232 4.8 7.7 1.0 CA A:SER232 4.8 7.7 1.0 CE A:LYS205 4.8 13.8 1.0 CB A:GLU233 4.9 7.5 1.0 CE1 A:HIS234 5.0 8.0 1.0 ND1 A:HIS234 5.0 8.0 1.0

Manganese binding site 2 out of 2 in the Structure of Plasmodium Falciparum Dxr in Complex with A Beta- Substituted Fosmidomycin Analogue, LC51 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, LC51 and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:7.2 occ:1.00 OE1 B:GLU233 2.1 8.1 1.0 OE2 B:GLU315 2.1 7.2 1.0 OD1 B:ASP231 2.1 7.6 1.0 O12 B:LC5501 2.2 8.6 1.0 O10 B:LC5501 2.2 9.0 1.0 OE2 B:GLU233 2.7 8.8 1.0 CD B:GLU233 2.7 7.6 1.0 C4 B:LC5501 2.9 9.9 1.0 N9 B:LC5501 2.9 9.5 1.0 CD B:GLU315 3.1 6.9 1.0 CG B:ASP231 3.1 7.6 1.0 OE1 B:GLU315 3.5 7.4 1.0 OD2 B:ASP231 3.5 7.6 1.0 NZ B:LYS205 3.6 12.5 1.0 O B:HOH717 3.7 18.7 1.0 OG B:SER232 3.8 7.2 1.0 N B:SER232 4.0 7.0 1.0 O B:HOH602 4.1 18.4 1.0 CG B:GLU233 4.2 7.5 1.0 ND2 B:ASN311 4.2 7.7 1.0 C3 B:LC5501 4.3 10.2 1.0 CG B:GLU315 4.3 6.7 1.0 C11 B:LC5501 4.3 9.7 1.0 CB B:ASP231 4.4 7.4 1.0 N B:GLU233 4.4 6.8 1.0 C B:ASP231 4.6 7.3 1.0 C2 B:LC5501 4.6 10.7 1.0 NZ B:LYS312 4.7 8.3 1.0 CA B:ASP231 4.7 7.3 1.0 CB B:SER232 4.8 7.0 1.0 CE B:LYS205 4.8 12.8 1.0 CA B:SER232 4.8 7.0 1.0 CB B:GLU233 4.8 7.1 1.0 CE1 B:HIS234 5.0 6.9 1.0 ND1 B:HIS234 5.0 6.7 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