Magnesium in PDB 6hft: HSP90 Co-Chaperone CNS1 From Saccharomyces Cerevisiae (DELTA69)

The structure of HSP90 Co-Chaperone CNS1 From Saccharomyces Cerevisiae (DELTA69), PDB code: 6hft was solved by E.M.Huber, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	50.780, 50.780, 283.070, 90.00, 90.00, 90.00
R / Rfree (%)	25.9 / 28.8

The binding sites of Magnesium atom in the HSP90 Co-Chaperone CNS1 From Saccharomyces Cerevisiae (DELTA69) (pdb code 6hft). 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 HSP90 Co-Chaperone CNS1 From Saccharomyces Cerevisiae (DELTA69), PDB code: 6hft:

Magnesium binding site 1 out of 1 in the HSP90 Co-Chaperone CNS1 From Saccharomyces Cerevisiae (DELTA69)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of HSP90 Co-Chaperone CNS1 From Saccharomyces Cerevisiae (DELTA69) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:58.8 occ:1.00 O A:LEU343 2.5 75.2 1.0 O A:LYS345 2.6 82.0 1.0 OD1 A:ASP349 2.8 82.6 1.0 O A:ASN235 3.2 74.2 1.0 ND2 A:ASN235 3.2 84.2 1.0 O A:LYS344 3.6 72.7 1.0 C A:LEU343 3.6 69.8 1.0 C A:LYS345 3.7 84.7 1.0 C A:LYS344 3.7 72.8 1.0 CG A:ASP349 3.8 84.3 1.0 N A:LYS345 4.1 75.2 1.0 CA A:LYS344 4.3 71.2 1.0 CG A:ASN235 4.3 81.4 1.0 CA A:ASP349 4.3 83.2 1.0 N A:LYS344 4.3 69.8 1.0 C A:ASN235 4.4 74.2 1.0 N A:VAL350 4.4 78.2 1.0 CA A:LYS345 4.5 80.3 1.0 CB A:ASP349 4.5 84.6 1.0 O A:VAL350 4.6 69.3 1.0 CA A:LEU343 4.6 66.5 1.0 N A:GLU346 4.6 90.5 1.0 OG1 A:THR237 4.7 91.8 1.0 CB A:ASN235 4.7 77.8 1.0 OD2 A:ASP349 4.7 85.5 1.0 C A:ASP349 4.8 81.7 1.0 CA A:GLU346 4.8 93.7 1.0 O A:ILE342 5.0 69.5 1.0

F.H.Schopf, E.M.Huber, C.Dodt, A.Lopez, M.M.Biebl, D.A.Rutz, M.Muhlhofer, G.Richter, T.Madl, M.Sattler, M.Groll, J.Buchner. The Co-Chaperone CNS1 and the Recruiter Protein HGH1 Link HSP90 to Translation Elongation Via Chaperoning Elongation Factor 2. Mol.Cell V. 74 73 2019.
ISSN: ISSN 1097-2765
PubMed: 30876805
DOI: 10.1016/J.MOLCEL.2019.02.011