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Atomistry » Sodium » PDB 2uzz-2vrp » 2vqr | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 2uzz-2vrp » 2vqr » |
Sodium in PDB 2vqr: Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase SuperfamilyProtein crystallography data
The structure of Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily, PDB code: 2vqr
was solved by
S.Jonas,
M.Hyvonen,
F.Hollfelder,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2vqr:
The structure of Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily
(pdb code 2vqr). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily, PDB code: 2vqr: Sodium binding site 1 out of 1 in 2vqrGo back to![]() ![]()
Sodium binding site 1 out
of 1 in the Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily
![]() Mono view ![]() Stereo pair view
Reference:
S.Jonas,
B.Van Loo,
M.Hyvonen,
F.Hollfelder.
A New Member of the Alkaline Phosphatase Superfamily with A Formylglycine Nucleophile: Structural and Kinetic Characterisation of A Phosphonate Monoester Hydrolase/Phosphodiesterase From Rhizobium Leguminosarum. J.Mol.Biol. V. 384 120 2008.
Page generated: Mon Oct 7 04:30:16 2024
ISSN: ISSN 0022-2836 PubMed: 18793651 DOI: 10.1016/J.JMB.2008.08.072 |
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