Magnesium in PDB 1qqn: D206S Mutant of Bovine 70 Kilodalton Heat Shock Protein

The structure of D206S Mutant of Bovine 70 Kilodalton Heat Shock Protein, PDB code: 1qqn was solved by E.R.Johnson, D.B.Mckay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	143.768, 64.424, 46.486, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 22.9

The structure of D206S Mutant of Bovine 70 Kilodalton Heat Shock Protein also contains other interesting chemical elements:

Potassium	(K)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Magnesium atom in the D206S Mutant of Bovine 70 Kilodalton Heat Shock Protein (pdb code 1qqn). 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 D206S Mutant of Bovine 70 Kilodalton Heat Shock Protein, PDB code: 1qqn:

Magnesium binding site 1 out of 1 in the D206S Mutant of Bovine 70 Kilodalton Heat Shock Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of D206S Mutant of Bovine 70 Kilodalton Heat Shock Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg487 b:12.5 occ:1.00 O A:HOH563 2.0 23.4 1.0 O A:HOH560 2.0 17.6 1.0 O A:HOH562 2.0 12.2 1.0 O2 A:PO4488 2.1 13.2 1.0 O A:HOH561 2.2 11.6 1.0 O2B A:ADP486 2.3 26.9 1.0 P A:PO4488 3.4 14.4 1.0 O3 A:PO4488 3.5 13.3 1.0 K A:K490 3.6 20.2 1.0 O A:HOH837 3.7 21.7 1.0 PB A:ADP486 3.8 26.9 1.0 K A:K491 3.9 29.4 1.0 OD1 A:ASP199 4.1 11.6 1.0 OD2 A:ASP199 4.2 11.2 1.0 OE2 A:GLU175 4.3 11.6 1.0 O4 A:PO4488 4.3 14.1 1.0 O3B A:ADP486 4.4 27.3 1.0 O1 A:PO4488 4.4 14.2 1.0 OD1 A:ASP10 4.5 8.5 1.0 CG A:ASP199 4.5 11.5 1.0 O A:HOH832 4.5 10.1 1.0 O3A A:ADP486 4.6 28.4 1.0 OD2 A:ASP10 4.6 8.2 1.0 O1B A:ADP486 4.7 27.4 1.0 PA A:ADP486 4.8 28.1 1.0 O A:HOH551 4.8 4.4 1.0 O A:HOH538 5.0 20.3 1.0 CD A:GLU175 5.0 11.4 1.0

E.R.Johnson, D.B.Mckay. Mapping the Role of Active Site Residues For Transducing An Atp-Induced Conformational Change in the Bovine 70-kDa Heat Shock Cognate Protein. Biochemistry V. 38 10823 1999.
ISSN: ISSN 0006-2960
PubMed: 10451379
DOI: 10.1021/BI990816G