Magnesium in PDB 3ehf: Crystal Structure of Deskc in Complex with Amp-Pcp

All present enzymatic activity of Crystal Structure of Deskc in Complex with Amp-Pcp:
2.7.13.3;

The structure of Crystal Structure of Deskc in Complex with Amp-Pcp, PDB code: 3ehf was solved by D.Albanesi, P.M.Alzari, A.Buschiazzo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 3.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	75.800, 44.700, 131.450, 90.00, 103.00, 90.00
R / Rfree (%)	24.2 / 29.7

The binding sites of Magnesium atom in the Crystal Structure of Deskc in Complex with Amp-Pcp (pdb code 3ehf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Deskc in Complex with Amp-Pcp, PDB code: 3ehf:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Deskc in Complex with Amp-Pcp


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 Deskc in Complex with Amp-Pcp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:64.1 occ:1.00 OE2 A:GLU289 2.0 62.1 1.0 O1A A:ACP500 2.1 64.5 1.0 O3G A:ACP500 2.1 73.8 1.0 O A:HOH1 2.1 14.4 1.0 O2B A:ACP500 2.1 71.3 1.0 OD1 A:ASN293 2.1 60.7 1.0 CG A:ASN293 2.8 57.1 1.0 ND2 A:ASN293 3.0 58.1 1.0 PB A:ACP500 3.2 76.8 1.0 CD A:GLU289 3.3 61.9 1.0 PA A:ACP500 3.3 68.6 1.0 PG A:ACP500 3.4 80.2 1.0 O3A A:ACP500 3.6 75.0 1.0 C3B A:ACP500 3.8 80.2 1.0 OE1 A:GLU289 4.1 63.7 1.0 CB A:ASN293 4.2 54.5 1.0 CG A:GLU289 4.3 60.2 1.0 O1G A:ACP500 4.3 82.4 1.0 O5' A:ACP500 4.4 66.7 1.0 O2A A:ACP500 4.4 72.3 1.0 O2G A:ACP500 4.5 83.0 1.0 CA A:GLY336 4.5 70.4 1.0 O1B A:ACP500 4.6 79.3 1.0 NE2 A:HIS297 4.6 63.9 1.0 CA A:ASN293 4.7 53.6 1.0 O A:GLU289 4.7 53.3 1.0 N A:GLY336 4.9 74.7 1.0 N A:ASN293 4.9 52.2 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Deskc in Complex with Amp-Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Deskc in Complex with Amp-Pcp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:90.9 occ:1.00 OE2 B:GLU289 2.0 85.4 1.0 O2B B:ACP500 2.0 98.0 1.0 O3G B:ACP500 2.1 95.6 1.0 O1A B:ACP500 2.1 96.9 1.0 CD B:GLU289 3.1 85.0 1.0 PB B:ACP500 3.2 0.5 1.0 PG B:ACP500 3.3 0.1 1.0 PA B:ACP500 3.4 0.3 1.0 C3B B:ACP500 3.6 0.5 1.0 CG B:GLU289 3.6 86.5 1.0 O3A B:ACP500 3.7 0.9 1.0 O1G B:ACP500 4.1 0.8 1.0 OE1 B:GLU289 4.2 83.7 1.0 CB B:ASN293 4.4 83.0 1.0 O2G B:ACP500 4.5 0.7 1.0 O1B B:ACP500 4.6 0.3 1.0 O2A B:ACP500 4.7 0.8 1.0 CG2 B:THR292 4.7 78.5 1.0 O B:GLU289 4.7 78.1 1.0 CA B:ASN293 4.9 79.9 1.0 N B:ASN293 4.9 77.0 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Deskc in Complex with Amp-Pcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Deskc in Complex with Amp-Pcp within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg501 b:73.3 occ:1.00 O D:HOH3 2.0 18.1 1.0 O2B D:ACP500 2.0 83.1 1.0 OE2 D:GLU289 2.1 66.6 1.0 O1A D:ACP500 2.1 75.4 1.0 OD1 D:ASN293 2.1 67.2 1.0 O3G D:ACP500 2.1 86.5 1.0 CG D:ASN293 2.9 63.6 1.0 ND2 D:ASN293 3.1 64.5 1.0 PB D:ACP500 3.2 91.2 1.0 CD D:GLU289 3.2 63.5 1.0 PA D:ACP500 3.2 81.2 1.0 O3A D:ACP500 3.3 88.3 1.0 PG D:ACP500 3.5 95.3 1.0 OE1 D:GLU289 3.8 64.7 1.0 C3B D:ACP500 4.0 96.3 1.0 CA D:GLY336 4.1 71.4 1.0 O5' D:ACP500 4.3 79.7 1.0 O1G D:ACP500 4.3 97.1 1.0 CB D:ASN293 4.4 59.6 1.0 O2A D:ACP500 4.4 83.2 1.0 CG D:GLU289 4.4 60.1 1.0 O1B D:ACP500 4.5 95.0 1.0 NE2 D:HIS297 4.5 73.2 1.0 O2G D:ACP500 4.6 97.8 1.0 N D:GLY336 4.6 77.6 1.0 O D:GLU289 4.7 55.1 1.0 CD2 D:HIS297 4.8 69.0 1.0 CA D:ASN293 4.9 59.0 1.0 C D:GLY336 5.0 69.1 1.0

D.Albanesi, M.Martin, F.Trajtenberg, M.C.Mansilla, A.Haouz, P.M.Alzari, D.De Mendoza, A.Buschiazzo. Structural Plasticity and Catalysis Regulation of A Thermosensor Histidine Kinase Proc.Natl.Acad.Sci.Usa V. 106 16185 2009.
ISSN: ISSN 0027-8424
PubMed: 19805278
DOI: 10.1073/PNAS.0906699106