Magnesium in PDB 3dzo: Crystal Structure of A Rhoptry Kinase From Toxoplasma Gondii

The structure of Crystal Structure of A Rhoptry Kinase From Toxoplasma Gondii, PDB code: 3dzo was solved by A.K.Wernimont, A.Lam, A.Ali, Y.H.Lin, S.Ni, M.Ravichandran, G.Wasney, M.Vedadi, I.Kozieradzki, M.Schapira, A.Bochkarev, M.Wilkstrom, C.Bountra, C.H.Arrowsmith, A.M.Edwards, D.Sibley, R.Hui, W.Qiu, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.261, 44.288, 105.304, 90.00, 98.90, 90.00
R / Rfree (%)	24.4 / 27

The binding sites of Magnesium atom in the Crystal Structure of A Rhoptry Kinase From Toxoplasma Gondii (pdb code 3dzo). 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 A Rhoptry Kinase From Toxoplasma Gondii, PDB code: 3dzo:

Magnesium binding site 1 out of 1 in the Crystal Structure of A Rhoptry Kinase From Toxoplasma Gondii


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 A Rhoptry Kinase From Toxoplasma Gondii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:47.0 occ:1.00 O A:HOH115 1.8 43.0 1.0 O A:HOH113 2.1 44.1 1.0 O A:HOH114 2.1 48.1 1.0 OE2 A:GLU433 2.2 31.5 1.0 CD A:GLU433 3.3 32.4 1.0 O A:HOH27 3.5 39.6 1.0 OE1 A:GLU433 3.8 32.7 1.0 OD2 A:ASP418 4.0 34.8 1.0 NH2 A:ARG415 4.1 33.2 1.0 OD1 A:ASP418 4.1 33.2 1.0 NE2 A:HIS434 4.3 33.8 1.0 CD2 A:HIS434 4.4 33.3 1.0 CG A:GLU433 4.5 31.3 1.0 CG A:ASP418 4.5 32.5 1.0 O A:GLY431 4.6 30.0 1.0 O A:HOH130 4.8 51.4 1.0 CA A:GLY431 4.8 30.3 1.0

W.Qiu, A.Wernimont, K.Tang, S.Taylor, V.Lunin, M.Schapira, S.Fentress, R.Hui, L.D.Sibley. Novel Structural and Regulatory Features of Rhoptry Secretory Kinases in Toxoplasma Gondii. Embo J. V. 28 969 2009.
ISSN: ISSN 0261-4189
PubMed: 19197235
DOI: 10.1038/EMBOJ.2009.24