Atomistry » Magnesium » PDB 1mum-1n6i » 1n57
Atomistry »
  Magnesium »
    PDB 1mum-1n6i »
      1n57 »

Magnesium in PDB 1n57: Crystal Structure of Chaperone HSP31

Protein crystallography data

The structure of Crystal Structure of Chaperone HSP31, PDB code: 1n57 was solved by P.M.Quigley, K.Korotkov, F.Baneyx, W.G.J.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.73 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 52.150, 82.000, 64.480, 90.00, 100.00, 90.00
R / Rfree (%) 18.7 / 24.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Chaperone HSP31 (pdb code 1n57). 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 Crystal Structure of Chaperone HSP31, PDB code: 1n57:

Magnesium binding site 1 out of 1 in 1n57

Go back to Magnesium Binding Sites List in 1n57
Magnesium binding site 1 out of 1 in the Crystal Structure of Chaperone HSP31


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Chaperone HSP31 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2252

b:14.0
occ:1.00
O A:HOH1237 2.0 13.4 1.0
O A:HOH1238 2.0 17.2 1.0
O A:HOH1235 2.1 15.8 1.0
O A:HOH1236 2.2 30.6 1.0
O A:HOH1143 4.3 20.4 1.0
O A:GLU219 4.5 13.2 1.0
O A:HOH1142 4.6 21.0 1.0
O A:HOH1346 4.8 28.4 1.0
CA A:GLU219 5.0 12.4 1.0

Reference:

P.M.Quigley, K.Korotkov, F.Baneyx, W.G.J.Hol. The 1.6A Crystal Structure of the Class of Chaperone Represented By Escherichia Coli HSP31 Reveals A Putative Catalytic Triad Proc.Natl.Acad.Sci.Usa V. 100 3137 2003.
ISSN: ISSN 0027-8424
PubMed: 12621151
DOI: 10.1073/PNAS.0530312100
Page generated: Tue Aug 13 09:22:04 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy