Magnesium in PDB 6gpw: Structure of Human Heat Shock Protein 90-Alpha N-Terminal Domain (HSP90-Ntd)

The structure of Structure of Human Heat Shock Protein 90-Alpha N-Terminal Domain (HSP90-Ntd), PDB code: 6gpw was solved by G.Tassone, C.Pozzi, S.Mangani, M.Botta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.45 / 1.60
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	65.040, 88.890, 100.050, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 19.9

The structure of Structure of Human Heat Shock Protein 90-Alpha N-Terminal Domain (HSP90-Ntd) also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Structure of Human Heat Shock Protein 90-Alpha N-Terminal Domain (HSP90-Ntd) (pdb code 6gpw). 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 Structure of Human Heat Shock Protein 90-Alpha N-Terminal Domain (HSP90-Ntd), PDB code: 6gpw:

Magnesium binding site 1 out of 1 in the Structure of Human Heat Shock Protein 90-Alpha N-Terminal Domain (HSP90-Ntd)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Heat Shock Protein 90-Alpha N-Terminal Domain (HSP90-Ntd) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:31.4 occ:0.50 O A:HOH436 2.0 33.1 1.0 O A:HOH729 2.2 36.8 1.0 O A:HOH541 2.2 32.6 1.0 O A:HOH679 4.0 47.3 1.0 O A:HOH431 4.2 41.3 1.0 OD2 A:ASP54 4.3 20.7 1.0 O A:HOH725 4.4 38.4 1.0 OD1 A:ASP54 4.4 21.3 1.0 O A:HOH654 4.6 37.1 1.0 CG A:ASP54 4.8 19.6 1.0 O A:HOH639 4.9 40.7 1.0

G.Tassone, S.Mangani, M.Botta, C.Pozzi. Probing the Role of ARG97 in Heat Shock Protein 90 N-Terminal Domain From the Parasite Leishmania Braziliensis Through Site-Directed Mutagenesis on the Human Counterpart. Biochim Biophys Acta V.1866 1190 2018PROTEINS Proteom.
ISSN: ISSN 1878-1454
PubMed: 30248409
DOI: 10.1016/J.BBAPAP.2018.09.005