Magnesium in PDB 1ny5: Crystal Structure of SIGM54 Activator (Aaa+ Atpase) in the Inactive State

The structure of Crystal Structure of SIGM54 Activator (Aaa+ Atpase) in the Inactive State, PDB code: 1ny5 was solved by S.Y.Lee, A.De La Torre, S.Kustu, B.T.Nixon, D.E.Wemmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.62 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.765, 94.765, 195.010, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 25.7

The binding sites of Magnesium atom in the Crystal Structure of SIGM54 Activator (Aaa+ Atpase) in the Inactive State (pdb code 1ny5). 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 SIGM54 Activator (Aaa+ Atpase) in the Inactive State, PDB code: 1ny5:

Magnesium binding site 1 out of 1 in the Crystal Structure of SIGM54 Activator (Aaa+ Atpase) in the Inactive State


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 SIGM54 Activator (Aaa+ Atpase) in the Inactive State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:69.8 occ:1.00 O3B A:ADP604 2.3 37.5 1.0 O A:HOH761 3.0 71.1 1.0 PB A:ADP604 3.6 36.6 1.0 NH2 A:ARG357 3.7 60.5 1.0 OD2 A:ASP238 3.8 59.0 1.0 O A:HOH605 3.9 23.4 1.0 NZ A:LYS173 4.0 34.8 1.0 O2B A:ADP604 4.0 38.7 1.0 OE1 A:GLU239 4.0 78.4 1.0 O1B A:ADP604 4.3 37.2 1.0 NH1 A:ARG357 4.3 55.0 1.0 N A:GLY170 4.3 36.4 1.0 CB A:SER169 4.4 44.2 1.0 OD1 A:ASP238 4.4 47.8 1.0 CA A:SER169 4.4 40.4 1.0 CZ A:ARG357 4.5 56.6 1.0 CG A:ASP238 4.5 52.8 1.0 CE A:LYS173 4.7 34.3 1.0 O3A A:ADP604 4.8 40.0 1.0 CD A:GLU239 4.9 72.3 1.0 C A:SER169 4.9 39.0 1.0

S.Y.Lee, A.De La Torre, D.Yan, S.Kustu, B.T.Nixon, D.E.Wemmer. Regulation of the Transcriptional Activator NTRC1: Structural Studies of the Regulatory and Aaa+ Atpase Domains Genes Dev. V. 17 2552 2003.
ISSN: ISSN 0890-9369
PubMed: 14561776
DOI: 10.1101/GAD.1125603