Calcium in PDB 5v0s: Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis

All present enzymatic activity of Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis:
1.3.1.12;

The structure of Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis, PDB code: 5v0s was solved by I.G.Shabalin, J.Hou, M.T.Cymborowski, Z.Otwinowski, K.Kwon, D.Christendat, A.Gritsunov, W.F.Anderson, W.Minor, Center For Structural Genomics Ofinfectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.63 / 2.01
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	48.070, 48.070, 233.395, 90.00, 90.00, 120.00
R / Rfree (%)	17.1 / 23.2

The binding sites of Calcium atom in the Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis (pdb code 5v0s). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis, PDB code: 5v0s:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:85.6 occ:0.70 O A:HOH506 2.4 81.7 1.0 OE2 A:GLU331 2.4 0.2 1.0 OE1 A:GLU331 2.8 0.1 1.0 CD A:GLU331 2.9 0.3 1.0 CG A:GLU331 4.3 77.3 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Act Domain of Prephenate Dehydrogenase Tyra From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:80.9 occ:0.80 O B:HOH503 2.4 81.0 1.0 O B:ARG329 2.9 44.8 1.0 C B:ARG329 3.8 40.3 1.0 CA B:ARG329 4.0 43.8 1.0 CG B:ARG329 4.2 55.5 1.0 OE2 B:GLU331 4.3 0.7 1.0 CB B:ARG329 4.5 37.5 1.0 O B:ALA328 4.9 36.3 1.0

I.G.Shabalin, J.Hou, D.Christendat, W.Minor. The Crystal Structure of Bacillus Anthracis Prephenate Dehydrogenase Identified An Act Regulatory Domain and A Novel Mode of Metabolic Regulation For Proteins Within the Prephenate Dehydrogenase Family of Enzyme To Be Published.