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Atomistry » Sodium » PDB 4wxs-4xdu » 4xb2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 4wxs-4xdu » 4xb2 » |
Sodium in PDB 4xb2: Hyperthermophilic Archaeal Homoserine Dehydrogenase Mutant in Complex with NadphProtein crystallography data
The structure of Hyperthermophilic Archaeal Homoserine Dehydrogenase Mutant in Complex with Nadph, PDB code: 4xb2
was solved by
H.Sakuraba,
S.Inoue,
K.Yoneda,
T.Ohshima,
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 Hyperthermophilic Archaeal Homoserine Dehydrogenase Mutant in Complex with Nadph
(pdb code 4xb2). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Hyperthermophilic Archaeal Homoserine Dehydrogenase Mutant in Complex with Nadph, PDB code: 4xb2: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 4xb2Go back to Sodium Binding Sites List in 4xb2
Sodium binding site 1 out
of 2 in the Hyperthermophilic Archaeal Homoserine Dehydrogenase Mutant in Complex with Nadph
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 4xb2Go back to Sodium Binding Sites List in 4xb2
Sodium binding site 2 out
of 2 in the Hyperthermophilic Archaeal Homoserine Dehydrogenase Mutant in Complex with Nadph
Mono view Stereo pair view
Reference:
J.Hayashi,
S.Inoue,
K.Kim,
K.Yoneda,
Y.Kawarabayasi,
T.Ohshima,
H.Sakuraba.
Crystal Structures of A Hyperthermophilic Archaeal Homoserine Dehydrogenase Suggest A Novel Cofactor Binding Mode For Oxidoreductases Sci Rep V. 5 11674 2015.
Page generated: Tue Dec 15 09:44:25 2020
ISSN: ESSN 2045-2322 DOI: 10.1038/SREP11674 |
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