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Magnesium in PDB 4br7: Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex
Enzymatic activity of Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex
All present enzymatic activity of Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex:
3.6.1.5;
3.6.1.5;
Protein crystallography data
The structure of Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex, PDB code: 4br7
was solved by
M.Zebisch,
P.Schaefer,
P.Lauble,
N.Straeter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 27.61 / 1.80 |
| Space group | P 3 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 102.853, 102.853, 74.779, 90.00, 90.00, 120.00 |
| R / Rfree (%) | 16.3 / 20.9 |
Other elements in 4br7:
The structure of Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex also contains other interesting chemical elements:
| Chlorine | (Cl) | 2 atoms |
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex
(pdb code 4br7). 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 Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex, PDB code: 4br7:
In total only one binding site of Magnesium was determined in the Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex, PDB code: 4br7:
Magnesium binding site 1 out of 1 in 4br7
Go back to
Magnesium Binding Sites List in 4br7
Magnesium binding site 1 out
of 1 in the Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Legionella Pneumophila NTPDASE1 Crystal Form I, Open, Ampnp Complex within 5.0Å range:
|
Reference:
M.Zebisch,
M.Krauss,
P.Schaefer,
P.Lauble,
N.Straeter.
Crystallographic Snapshots Along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases Structure V. 21 1460 2013.
ISSN: ISSN 0969-2126
PubMed: 23830739
DOI: 10.1016/J.STR.2013.05.016
Page generated: Mon Dec 14 09:12:19 2020
ISSN: ISSN 0969-2126
PubMed: 23830739
DOI: 10.1016/J.STR.2013.05.016
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