Magnesium in PDB 1zy2: Crystal Structure of the Phosphorylated Receiver Domain of the Transcription Regulator NTRC1 From Aquifex Aeolicus

The structure of Crystal Structure of the Phosphorylated Receiver Domain of the Transcription Regulator NTRC1 From Aquifex Aeolicus, PDB code: 1zy2 was solved by M.Doucleff, B.Chen, A.E.Maris, D.E.Wemmer, E.Kondrashkina, B.T.Nixon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.00 / 3.03
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.517, 91.517, 130.942, 90.00, 90.00, 120.00
R / Rfree (%)	25.1 / 28.3

The binding sites of Magnesium atom in the Crystal Structure of the Phosphorylated Receiver Domain of the Transcription Regulator NTRC1 From Aquifex Aeolicus (pdb code 1zy2). 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 the Phosphorylated Receiver Domain of the Transcription Regulator NTRC1 From Aquifex Aeolicus, PDB code: 1zy2:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Phosphorylated Receiver Domain of the Transcription Regulator NTRC1 From Aquifex Aeolicus


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 the Phosphorylated Receiver Domain of the Transcription Regulator NTRC1 From Aquifex Aeolicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg151 b:0.4 occ:1.00 OP2 A:PHD51 2.9 0.8 1.0 OD2 A:ASP8 3.0 0.5 1.0 OD2 A:PHD51 3.3 78.2 1.0 O A:LEU53 3.5 0.3 1.0 OE2 A:GLU7 3.7 0.6 1.0 CG A:ASP8 3.8 63.1 1.0 OD1 A:ASP8 3.9 0.8 1.0 P A:PHD51 4.3 0.4 1.0 CG A:PHD51 4.4 70.4 1.0 CD1 A:LEU53 4.6 0.5 1.0 C A:LEU53 4.6 0.6 1.0 OD1 A:PHD51 4.8 0.3 1.0 CD A:GLU7 5.0 97.9 1.0 CB A:LEU53 5.0 76.1 1.0

M.Doucleff, B.Chen, A.E.Maris, D.E.Wemmer, E.Kondrashkina, B.T.Nixon. Negative Regulation of Aaa + Atpase Assembly By Two Component Receiver Domains: A Transcription Activation Mechanism That Is Conserved in Mesophilic and Extremely Hyperthermophilic Bacteria J.Mol.Biol. V. 353 242 2005.
ISSN: ISSN 0022-2836
PubMed: 16169010
DOI: 10.1016/J.JMB.2005.08.003