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Atomistry » Potassium » PDB 7o2p-7otj » 7ocr » |
Potassium in PDB 7ocr: Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter BaumanniiProtein crystallography data
The structure of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocr
was solved by
H.K.Tam,
V.Mueller,
K.M.Pos,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7ocr:
The structure of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii
(pdb code 7ocr). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocr: Potassium binding site 1 out of 1 in 7ocrGo back to Potassium Binding Sites List in 7ocr
Potassium binding site 1 out
of 1 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii
Mono view Stereo pair view
Reference:
H.K.Tam,
P.Konig,
S.Himpich,
N.D.Ngu,
R.Abele,
V.Muller,
K.M.Pos.
Unidirectional Mannitol Synthesis of Acinetobacter Baumannii Mtld Is Facilitated By the Helix-Loop-Helix-Mediated Dimer Formation. Proc.Natl.Acad.Sci.Usa V. 119 94119 2022.
Page generated: Mon Aug 12 19:38:37 2024
ISSN: ESSN 1091-6490 PubMed: 35363566 DOI: 10.1073/PNAS.2107994119 |
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