Magnesium in PDB 7myv: Plasmodium Falciparum HAD5/Pmm

All present enzymatic activity of Plasmodium Falciparum HAD5/Pmm:
5.4.2.8;

The structure of Plasmodium Falciparum HAD5/Pmm, PDB code: 7myv was solved by P.M.Frasse, A.R.Odom John, D.E.Goldberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.31 / 3.51
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	161.255, 161.255, 109.738, 90, 90, 120
R / Rfree (%)	25.4 / 30.7

The binding sites of Magnesium atom in the Plasmodium Falciparum HAD5/Pmm (pdb code 7myv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Plasmodium Falciparum HAD5/Pmm, PDB code: 7myv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Plasmodium Falciparum HAD5/Pmm


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Plasmodium Falciparum HAD5/Pmm within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:75.9 occ:1.00 OD2 A:ASP14 2.1 91.4 1.0 O A:ASP16 2.4 102.6 1.0 OD2 A:ASP210 2.7 105.1 1.0 CG A:ASP14 3.1 97.3 1.0 CG A:ASP210 3.4 102.0 1.0 OD1 A:ASP14 3.5 101.7 1.0 C A:ASP16 3.6 101.8 1.0 CB A:ASP210 3.6 102.5 1.0 CB A:ASP14 4.3 98.1 1.0 CA A:ASP16 4.5 95.9 1.0 OD1 A:ASP210 4.5 105.9 1.0 CB A:ASP16 4.5 94.8 1.0 N A:GLY17 4.5 100.6 1.0 CA A:GLY17 4.6 96.6 1.0 N A:ASP16 4.6 96.3 1.0 N A:ASP210 4.7 103.7 1.0 CA A:ASP210 4.8 102.7 1.0 OD2 A:ASP218 4.9 105.1 1.0 OG1 A:THR18 4.9 96.6 1.0 N A:THR18 5.0 94.0 1.0

Magnesium binding site 2 out of 2 in the Plasmodium Falciparum HAD5/Pmm


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Plasmodium Falciparum HAD5/Pmm within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg500 b:65.3 occ:1.00 OD2 B:ASP14 1.9 100.9 1.0 OD1 B:ASP210 2.4 92.1 1.0 OD2 B:ASP210 2.6 72.6 1.0 CG B:ASP210 2.6 80.2 1.0 CG B:ASP14 2.7 96.8 1.0 O B:ASP16 2.7 85.7 1.0 OD1 B:ASP14 2.8 107.4 1.0 CB B:ASP16 3.6 78.6 1.0 C B:ASP16 3.6 74.1 1.0 CB B:ASP210 3.9 72.0 1.0 CA B:ASP16 4.0 68.9 1.0 CB B:ASP14 4.1 84.0 1.0 N B:ASP16 4.2 69.8 1.0 ND2 B:ASN217 4.3 92.8 1.0 OD1 B:ASN217 4.4 86.9 1.0 OD1 B:ASP218 4.5 83.8 1.0 N B:ASP210 4.7 81.5 1.0 N B:GLY17 4.7 66.5 1.0 CG B:ASN217 4.8 89.3 1.0 CA B:ASP210 4.8 80.2 1.0 CG B:ASP16 4.9 79.1 1.0 OD2 B:ASP218 4.9 86.9 1.0 N B:ARG211 5.0 82.0 1.0

P.M.Frasse, J.J.Miller, A.J.Polino, E.Soleimani, J.S.Zhu, D.L.Jakeman, J.M.Jez, D.E.Goldberg, A.R.Odom John. Enzymatic and Structural Characterization of HAD5, An Essential Phosphomannomutase of Malaria-Causing Parasites. J.Biol.Chem. V. 298 01550 2022.
ISSN: ESSN 1083-351X
PubMed: 34973333
DOI: 10.1016/J.JBC.2021.101550