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Magnesium in PDB 1byq: HSP90 N-Terminal Domain Bound to Adp-Mg

Protein crystallography data

The structure of HSP90 N-Terminal Domain Bound to Adp-Mg, PDB code: 1byq was solved by A.A.Russo, N.P.Pavletich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.140, 42.500, 53.960, 90.00, 115.53, 90.00
R / Rfree (%) 18.9 / 24.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the HSP90 N-Terminal Domain Bound to Adp-Mg (pdb code 1byq). 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 Adp-Mg, PDB code: 1byq:

Magnesium binding site 1 out of 1 in 1byq

Go back to Magnesium Binding Sites List in 1byq
Magnesium binding site 1 out of 1 in the HSP90 N-Terminal Domain Bound to Adp-Mg


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 Adp-Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:13.1
occ:1.00
OD1 A:ASN51 2.1 10.4 1.0
O1B A:ADP2001 2.1 12.9 1.0
O1A A:ADP2001 2.1 11.2 1.0
O A:HOH2290 2.1 14.4 1.0
O A:HOH2291 2.2 13.6 1.0
O A:HOH2289 2.2 17.0 1.0
CG A:ASN51 3.1 11.6 1.0
PB A:ADP2001 3.3 13.5 1.0
PA A:ADP2001 3.3 10.4 1.0
O3A A:ADP2001 3.5 12.2 1.0
ND2 A:ASN51 3.5 9.0 1.0
O3B A:ADP2001 3.8 17.0 1.0
O A:HOH2012 3.9 14.0 1.0
O5' A:ADP2001 4.0 11.1 1.0
O A:HOH2187 4.1 40.2 1.0
OE1 A:GLU47 4.2 17.6 1.0
CB A:ASN51 4.4 9.0 1.0
O A:GLU47 4.4 10.4 1.0
O2B A:ADP2001 4.5 13.7 1.0
O2A A:ADP2001 4.5 8.8 1.0
OD2 A:ASP54 4.5 14.1 1.0
CA A:ASN51 4.6 6.0 1.0
N A:ASN51 4.7 7.4 1.0
CA A:GLY137 4.9 9.8 1.0
N A:PHE138 5.0 6.8 1.0

Reference:

W.M.Obermann, H.Sondermann, A.A.Russo, N.P.Pavletich, F.U.Hartl. In Vivo Function of HSP90 Is Dependent on Atp Binding and Atp Hydrolysis. J.Cell Biol. V. 143 901 1998.
ISSN: ISSN 0021-9525
PubMed: 9817749
DOI: 10.1083/JCB.143.4.901
Page generated: Sat Aug 9 20:14:33 2025

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