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Atomistry » Sodium » PDB 5gwl-5hn2 » 5hi0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 5gwl-5hn2 » 5hi0 » |
Sodium in PDB 5hi0: The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate DecarboxylaseEnzymatic activity of The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate Decarboxylase
All present enzymatic activity of The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate Decarboxylase:
4.1.1.2; Protein crystallography data
The structure of The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate Decarboxylase, PDB code: 5hi0
was solved by
W.Zhu,
L.M.Easthon,
L.A.Reinhardt,
C.Tu,
S.E.Cohen,
D.N.Silverman,
K.N.Allen,
N.G.J.Richards,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5hi0:
The structure of The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate Decarboxylase also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate Decarboxylase
(pdb code 5hi0). 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 The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate Decarboxylase, PDB code: 5hi0: Sodium binding site 1 out of 1 in 5hi0Go back to Sodium Binding Sites List in 5hi0
Sodium binding site 1 out
of 1 in the The Substrate Binding Mode and Chemical Basis of A Reaction Specificity Switch in Oxalate Decarboxylase
Mono view Stereo pair view
Reference:
W.Zhu,
L.M.Easthon,
L.A.Reinhardt,
C.Tu,
S.E.Cohen,
D.N.Silverman,
K.N.Allen,
N.G.Richards.
Substrate Binding Mode and Molecular Basis of A Specificity Switch in Oxalate Decarboxylase. Biochemistry V. 55 2163 2016.
Page generated: Mon Oct 7 21:23:58 2024
ISSN: ISSN 0006-2960 PubMed: 27014926 DOI: 10.1021/ACS.BIOCHEM.6B00043 |
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