Atomistry » Magnesium » PDB 2g9z-2gqp » 2glq
Atomistry »
  Magnesium »
    PDB 2g9z-2gqp »
      2glq »

Magnesium in PDB 2glq: X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium

Enzymatic activity of X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium

All present enzymatic activity of X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium:
3.1.3.1;

Protein crystallography data

The structure of X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium, PDB code: 2glq was solved by P.Llinas, M.Masella, T.Stigbrand, A.Menez, E.A.Stura, M.H.Le Du, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.99 / 1.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.090, 115.299, 107.320, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 18.8

Other elements in 2glq:

The structure of X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium also contains other interesting chemical elements:

Strontium (Sr) 1 atom
Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium (pdb code 2glq). 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 X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium, PDB code: 2glq:

Magnesium binding site 1 out of 1 in 2glq

Go back to Magnesium Binding Sites List in 2glq
Magnesium binding site 1 out of 1 in the X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2003

b:12.6
occ:1.00
OD2 A:ASP42 2.0 10.9 1.0
O A:HOH2016 2.1 11.2 1.0
OE2 A:GLU311 2.1 12.4 1.0
O A:HOH2578 2.1 9.6 1.0
OG A:SER155 2.2 12.0 1.0
CG A:ASP42 3.0 12.0 1.0
CB A:SER155 3.1 11.6 1.0
CD A:GLU311 3.1 10.9 1.0
OE1 A:GLU311 3.5 12.7 1.0
CB A:ASP42 3.6 11.6 1.0
O A:HOH2015 4.0 11.7 1.0
OD1 A:ASP42 4.1 10.5 1.0
N A:SER155 4.1 12.7 1.0
CA A:SER155 4.2 12.4 1.0
OG A:SEP92 4.4 14.6 1.0
O3P A:SEP92 4.4 11.8 1.0
O A:HOH2039 4.4 12.2 1.0
CG A:GLU311 4.4 12.2 1.0
CD2 A:HIS153 4.4 19.4 1.0
CB A:SEP92 4.5 14.5 1.0
O A:GLY313 4.5 14.6 1.0
CG2 A:THR149 4.7 15.6 1.0
CA A:GLY313 4.7 13.4 1.0
ZN A:ZN2002 4.7 11.9 1.0
OD2 A:ASP357 4.8 10.2 1.0
CD A:PRO156 4.8 11.9 1.0
OG1 A:THR149 4.9 15.4 1.0
CA A:ASP42 5.0 11.2 1.0

Reference:

P.Llinas, M.Masella, T.Stigbrand, A.Menez, E.A.Stura, M.H.Le Du. Structural Studies of Human Alkaline Phosphatase in Complex with Strontium: Implication For Its Secondary Effect in Bones. Protein Sci. V. 15 1691 2006.
ISSN: ISSN 0961-8368
PubMed: 16815919
DOI: 10.1110/PS.062123806
Page generated: Tue Aug 13 23:31:50 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy