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Strontium 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:

Magnesium (Mg) 1 atom
Zinc (Zn) 2 atoms

Strontium Binding Sites:

The binding sites of Strontium 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 Strontium atom.
In total only one binding site of Strontium was determined in the X-Ray Structure of Human Alkaline Phosphatase in Complex with Strontium, PDB code: 2glq:

Strontium binding site 1 out of 1 in 2glq

Go back to Strontium Binding Sites List in 2glq
Strontium 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 Strontium with other atoms in the Sr 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:Sr2004

b:22.1
occ:1.00
 OE2 A:GLU270 2.4 25.3 1.0
OE1 A:GLU216 2.5 23.8 1.0
O A:HOH2119 2.5 19.9 1.0
O A:PHE269 2.5 17.2 1.0
OD2 A:ASP285 2.5 23.6 1.0
OE2 A:GLU216 2.5 26.5 1.0
O A:HOH2489 2.7 32.9 1.0
OD1 A:ASP285 2.8 30.3 1.0
CD A:GLU216 2.8 26.6 1.0
CG A:ASP285 3.0 23.5 1.0
CD A:GLU270 3.3 23.0 1.0
C A:PHE269 3.7 15.7 1.0
OE1 A:GLU270 4.0 21.9 1.0
O A:HOH2517 4.1 25.6 1.0
CG A:GLU270 4.1 17.9 1.0
CG A:GLU216 4.3 28.2 1.0
OH A:TYR217 4.4 32.8 1.0
O A:HOH2067 4.5 20.5 1.0
CB A:ASP285 4.5 21.1 1.0
CA A:PHE269 4.6 16.5 1.0
O A:LEU284 4.6 19.8 1.0
CB A:LEU284 4.6 22.3 1.0
N A:GLU270 4.6 16.2 1.0
CA A:GLU270 4.7 15.9 1.0
O A:HOH2293 4.7 34.1 1.0
CB A:PHE269 4.7 15.6 1.0
NH1 A:ARG204 4.7 17.9 1.0
NH2 A:ARG204 4.8 16.1 1.0
O A:TRP248 4.8 16.9 1.0
NZ A:LYS275 4.8 33.1 1.0
C A:LEU284 4.9 20.6 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: Thu Oct 10 20:58:50 2024

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