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Atomistry » Chlorine » PDB 7obe-7okc » 7ocu » |
Chlorine in PDB 7ocu: Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter BaumanniiProtein crystallography data
The structure of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter Baumannii, PDB code: 7ocu
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 7ocu:
The structure of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter Baumannii also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter Baumannii
(pdb code 7ocu). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter Baumannii, PDB code: 7ocu: Chlorine binding site 1 out of 1 in 7ocuGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A 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: Sun Jul 13 04:54:57 2025
ISSN: ESSN 1091-6490 PubMed: 35363566 DOI: 10.1073/PNAS.2107994119 |
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