Magnesium in PDB 3fcc: Crystal Structure of Dlta Protein in Complex with Atp and Magnesium

All present enzymatic activity of Crystal Structure of Dlta Protein in Complex with Atp and Magnesium:
6.1.1.13;

The structure of Crystal Structure of Dlta Protein in Complex with Atp and Magnesium, PDB code: 3fcc was solved by K.T.Osman, L.Du, Y.He, Y.Luo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.32
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.600, 87.000, 60.100, 90.00, 115.00, 90.00
R / Rfree (%)	24.1 / 28.6

The binding sites of Magnesium atom in the Crystal Structure of Dlta Protein in Complex with Atp and Magnesium (pdb code 3fcc). 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 Dlta Protein in Complex with Atp and Magnesium, PDB code: 3fcc:

Magnesium binding site 1 out of 1 in the Crystal Structure of Dlta Protein in Complex with Atp and Magnesium


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 Dlta Protein in Complex with Atp and Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg710 b:52.2 occ:1.00 O A:HOH791 2.1 68.9 1.0 O A:HOH793 2.3 45.2 1.0 O A:HOH792 2.4 46.7 1.0 O A:HOH794 2.4 46.3 1.0 O1G A:ATP711 2.5 46.8 1.0 O2B A:ATP711 3.0 42.5 1.0 PG A:ATP711 3.8 49.9 1.0 O3A A:ATP711 3.8 42.4 1.0 PB A:ATP711 3.9 41.0 1.0 O3B A:ATP711 4.4 45.9 1.0 OE2 A:GLU298 4.4 37.4 1.0 O2G A:ATP711 4.4 51.3 1.0 OH A:TYR379 4.4 32.3 1.0 O A:HOH844 4.4 60.2 1.0 NH1 A:ARG397 4.5 31.7 1.0 OE1 A:GLU298 4.6 38.7 1.0 O3' A:ATP711 4.8 27.0 1.0 O3G A:ATP711 4.8 50.3 1.0 CD A:GLU298 5.0 37.6 1.0 O A:THR381 5.0 35.5 1.0

K.T.Osman, L.Du, Y.He, Y.Luo. Crystal Structure of Bacillus Cereus D-Alanyl Carrier Protein Ligase (Dlta) in Complex with Atp. J.Mol.Biol. V. 388 345 2009.
ISSN: ISSN 0022-2836
PubMed: 19324056
DOI: 10.1016/J.JMB.2009.03.040