Magnesium in PDB 3hzt: Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860

All present enzymatic activity of Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860:
2.7.11.17;

The structure of Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860, PDB code: 3hzt was solved by A.K.Wernimont, J.D.Artz, P.Finnerty, G.Wasney, A.Allali-Hassani, M.Vedadi, A.Bochkarev, C.H.Arrowsmith, A.M.Edwards, C.Bountra, J.Weigelt, R.Hui, M.Amani, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	71.051, 43.761, 84.821, 90.00, 96.95, 90.00
R / Rfree (%)	20.7 / 25.2

The structure of Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860 (pdb code 3hzt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860, PDB code: 3hzt:

Magnesium binding site 1 out of 1 in the Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Toxoplasma Gondii CDPK3, TGME49_105860 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:44.6 occ:1.00 O A:HOH545 2.3 63.4 1.0 OD2 A:ASP398 2.3 60.2 1.0 OD1 A:ASP394 2.5 60.1 1.0 OD1 A:ASN396 2.5 60.9 1.0 OH A:TYR447 2.7 55.5 1.0 O A:GLN400 2.7 57.8 1.0 O A:HOH546 2.9 43.1 1.0 CG A:ASP398 3.2 60.1 1.0 CG A:ASN396 3.6 60.6 1.0 OD1 A:ASP398 3.6 60.8 1.0 CG A:ASP394 3.6 60.0 1.0 C A:GLN400 3.8 57.9 1.0 CZ A:TYR447 3.8 55.8 1.0 ND2 A:ASN396 4.0 59.4 1.0 N A:GLN400 4.2 58.7 1.0 CA A:ASP394 4.3 59.8 1.0 CE1 A:TYR447 4.3 56.0 1.0 N A:ASP398 4.4 59.9 1.0 CA A:GLN400 4.4 58.2 1.0 CB A:ASP394 4.5 59.7 1.0 OD2 A:ASP394 4.5 59.7 1.0 CB A:ASP398 4.5 59.8 1.0 N A:ASN396 4.6 60.2 1.0 C A:ASP394 4.6 59.8 1.0 N A:ASN395 4.6 59.9 1.0 CB A:GLN400 4.7 58.3 1.0 CD2 A:LEU401 4.7 55.6 1.0 N A:GLY397 4.8 60.3 1.0 CB A:ASN396 4.9 60.3 1.0 CA A:ASP398 4.9 59.6 1.0 N A:LEU401 4.9 57.9 1.0 OE2 A:GLU405 4.9 61.8 1.0 CE2 A:TYR447 4.9 55.9 1.0 N A:GLY399 4.9 59.2 1.0

A.K.Wernimont, J.D.Artz, P.Finerty, Y.H.Lin, M.Amani, A.Allali-Hassani, G.Senisterra, M.Vedadi, W.Tempel, F.Mackenzie, I.Chau, S.Lourido, L.D.Sibley, R.Hui. Structures of Apicomplexan Calcium-Dependent Protein Kinases Reveal Mechanism of Activation By Calcium. Nat.Struct.Mol.Biol. V. 17 596 2010.
ISSN: ISSN 1545-9993
PubMed: 20436473
DOI: 10.1038/NSMB.1795