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Atomistry » Sodium » PDB 2xjr-2xzi » 2xnj | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 2xjr-2xzi » 2xnj » |
Sodium in PDB 2xnj: Crystal Structure of An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia ColiEnzymatic activity of Crystal Structure of An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia Coli
All present enzymatic activity of Crystal Structure of An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia Coli:
1.18.1.2; Protein crystallography data
The structure of Crystal Structure of An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia Coli, PDB code: 2xnj
was solved by
H.Botti,
M.A.Musumeci,
E.A.Ceccarelli,
A.Buschiazzo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2xnj:
The structure of Crystal Structure of An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia Coli also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia Coli
(pdb code 2xnj). 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 An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia Coli, PDB code: 2xnj: Sodium binding site 1 out of 1 in 2xnjGo back to Sodium Binding Sites List in 2xnj
Sodium binding site 1 out
of 1 in the Crystal Structure of An Engineered Ferredoxin(Flavodoxin) Nadp(H) Reductase (Fpr) From Escherichia Coli
Mono view Stereo pair view
Reference:
M.A.Musumeci,
H.Botti,
A.Buschiazzo,
E.A.Ceccarelli.
Swapping Fad Binding Motifs Between Plastidic and Bacterial Ferredoxin-Nadp(H) Reductases. Biochemistry V. 50 2111 2011.
Page generated: Mon Oct 7 05:15:07 2024
ISSN: ISSN 0006-2960 PubMed: 21306142 DOI: 10.1021/BI101772A |
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