Potassium in PDB 1qqo: E175S Mutant of Bovine 70 Kilodalton Heat Shock Protein

The structure of E175S Mutant of Bovine 70 Kilodalton Heat Shock Protein, PDB code: 1qqo 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 (°)	143.756, 64.029, 46.406, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 23.9

The structure of E175S Mutant of Bovine 70 Kilodalton Heat Shock Protein also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Chlorine	(Cl)	2 atoms

The binding sites of Potassium atom in the E175S Mutant of Bovine 70 Kilodalton Heat Shock Protein (pdb code 1qqo). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the E175S Mutant of Bovine 70 Kilodalton Heat Shock Protein, PDB code: 1qqo:

Potassium binding site 1 out of 1 in the E175S Mutant of Bovine 70 Kilodalton Heat Shock Protein


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of E175S Mutant of Bovine 70 Kilodalton Heat Shock Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:K490 b:24.7 occ:1.00 O A:HOH558 2.5 9.5 1.0 O A:TYR15 2.8 9.5 1.0 OD1 A:ASP10 3.0 12.6 1.0 O A:HOH823 3.1 18.7 1.0 O A:HOH562 3.2 22.4 1.0 O3B A:ADP486 3.4 19.6 1.0 CG A:ASP10 3.4 11.9 1.0 O2B A:ADP486 3.4 20.8 1.0 OD2 A:ASP10 3.5 12.3 1.0 MG A:MG487 3.5 16.7 1.0 O3A A:ADP486 3.6 19.6 1.0 C A:TYR15 3.6 9.0 1.0 PB A:ADP486 3.7 19.1 1.0 CA A:GLY12 3.8 7.4 1.0 PA A:ADP486 3.9 17.9 1.0 O2A A:ADP486 4.0 20.4 1.0 N A:GLY12 4.2 7.4 1.0 CB A:TYR15 4.3 9.4 1.0 N A:SER16 4.4 9.1 1.0 CA A:SER16 4.4 8.9 1.0 CA A:TYR15 4.4 9.1 1.0 CB A:ASP10 4.6 10.8 1.0 O A:ASP10 4.6 8.6 1.0 O A:ASP366 4.6 9.3 1.0 N A:TYR15 4.7 8.4 1.0 O A:HOH566 4.7 7.1 1.0 C A:SER16 4.9 9.1 1.0 O A:HOH560 4.9 11.3 1.0 C A:GLY12 4.9 7.5 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