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Atomistry » Sodium » PDB 5b15-5bph » 5b4t » |
Sodium in PDB 5b4t: Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Alcaligenes Faecalis Complexed with Nad+ and A Substrate D-3- HydroxybutyrateEnzymatic activity of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Alcaligenes Faecalis Complexed with Nad+ and A Substrate D-3- Hydroxybutyrate
All present enzymatic activity of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Alcaligenes Faecalis Complexed with Nad+ and A Substrate D-3- Hydroxybutyrate:
1.1.1.30; Protein crystallography data
The structure of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Alcaligenes Faecalis Complexed with Nad+ and A Substrate D-3- Hydroxybutyrate, PDB code: 5b4t
was solved by
H.Kanazawa,
M.Tsunoda,
M.M.Hoque,
K.Suzuki,
T.Yamamoto,
A.Takenaka,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Alcaligenes Faecalis Complexed with Nad+ and A Substrate D-3- Hydroxybutyrate
(pdb code 5b4t). 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 D-3-Hydroxybutyrate Dehydrogenase From Alcaligenes Faecalis Complexed with Nad+ and A Substrate D-3- Hydroxybutyrate, PDB code: 5b4t: Sodium binding site 1 out of 1 in 5b4tGo back to Sodium Binding Sites List in 5b4t
Sodium binding site 1 out
of 1 in the Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Alcaligenes Faecalis Complexed with Nad+ and A Substrate D-3- Hydroxybutyrate
Mono view Stereo pair view
Reference:
H.Kanazawa,
M.M.Hoque,
M.Tsunoda,
K.Suzuki,
T.Yamamoto,
G.Kawai,
J.Kondo,
A.Takenaka.
Structural Insights Into the Catalytic Reaction Trigger and Inhibition of D-3-Hydroxybutyrate Dehydrogenase Acta Crystallogr.,Sect.F V. 72 507 2016.
Page generated: Mon Oct 7 20:03:20 2024
ISSN: ESSN 2053-230X PubMed: 27380367 DOI: 10.1107/S2053230X16007767 |
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