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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 3hzt:

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

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

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 3hzt

Go back to Magnesium Binding Sites List in 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

Reference:

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
Page generated: Mon Dec 14 08:15:17 2020

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