Magnesium in PDB 3t0z: HSP90 N-Terminal Domain Bound to Atp

The structure of HSP90 N-Terminal Domain Bound to Atp, PDB code: 3t0z was solved by J.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.49 / 2.19
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.709, 46.780, 53.223, 90.00, 111.59, 90.00
R / Rfree (%)	20.1 / 25.8

The binding sites of Magnesium atom in the HSP90 N-Terminal Domain Bound to Atp (pdb code 3t0z). 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 N-Terminal Domain Bound to Atp, PDB code: 3t0z:

Magnesium binding site 1 out of 1 in the HSP90 N-Terminal Domain Bound to Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of HSP90 N-Terminal Domain Bound to Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:16.1 occ:1.00 OD1 A:ASN51 2.2 15.0 1.0 O3G A:ATP301 2.2 11.9 1.0 O A:HOH556 2.2 13.2 1.0 O1A A:ATP301 2.3 13.9 1.0 O2B A:ATP301 2.3 12.0 1.0 O A:HOH584 2.4 25.2 1.0 CG A:ASN51 3.0 14.8 1.0 PB A:ATP301 3.4 10.5 1.0 ND2 A:ASN51 3.4 12.7 1.0 PG A:ATP301 3.4 17.3 1.0 PA A:ATP301 3.5 14.4 1.0 O3A A:ATP301 3.6 15.2 1.0 O3B A:ATP301 3.8 18.5 1.0 O1G A:ATP301 4.0 14.5 1.0 O A:GLU47 4.0 13.7 1.0 O A:HOH564 4.0 23.2 1.0 O A:HOH527 4.1 16.4 1.0 OE1 A:GLU47 4.2 16.1 1.0 O5' A:ATP301 4.3 14.1 1.0 CB A:ASN51 4.3 11.8 1.0 CA A:GLY137 4.5 12.4 1.0 N A:ASN51 4.5 13.6 1.0 CA A:ASN51 4.6 14.6 1.0 N A:PHE138 4.6 11.2 1.0 O2G A:ATP301 4.6 17.6 1.0 O2A A:ATP301 4.7 14.8 1.0 N A:GLY137 4.7 13.9 1.0 O1B A:ATP301 4.8 12.5 1.0 OD2 A:ASP54 4.8 24.6 1.0 C A:GLY137 4.8 13.2 1.0 CB A:SER50 5.0 16.9 1.0

J.Li, L.Sun, C.Xu, F.Yu, H.Zhou, Y.Zhao, J.Zhang, J.Cai, C.Mao, L.Tang, Y.Xu, J.He. Structure Insights Into Mechanisms of Atp Hydrolysis and the Activation of Human Heat-Shock Protein 90. Acta Biochim Biophys Sin V. 44 300 2012(Shanghai).
ISSN: ISSN 1672-9145
PubMed: 22318716
DOI: 10.1093/ABBS/GMS001