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Magnesium in PDB 7ocs: Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii

Protein crystallography data

The structure of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii, PDB code: 7ocs 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:

Resolution Low / High (Å) 48.61 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 88.888, 212.626, 98.819, 90, 112.81, 90
R / Rfree (%) 21.5 / 24.7

Other elements in 7ocs:

The structure of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii also contains other interesting chemical elements:

Chlorine (Cl) 10 atoms
Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii (pdb code 7ocs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii, PDB code: 7ocs:

Magnesium binding site 1 out of 1 in 7ocs

Go back to Magnesium Binding Sites List in 7ocs
Magnesium 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-D16A From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg815

b:66.8
occ:1.00
O A:THR412 2.7 36.9 1.0
O A:LEU373 2.8 51.7 1.0
O A:HOH991 2.9 31.4 1.0
OD1 A:ASP411 3.0 45.6 1.0
O2 A:SO4812 3.1 35.7 0.8
N A:THR412 3.7 35.9 1.0
C A:THR412 3.8 37.0 1.0
O A:ILE371 3.8 42.7 1.0
C A:LEU373 3.9 51.6 1.0
N A:LEU373 4.0 47.5 1.0
CB A:ALA378 4.0 62.3 1.0
CG A:ASP411 4.0 44.8 1.0
OG1 A:THR412 4.1 36.5 1.0
CA A:THR412 4.2 36.0 1.0
O A:LYS375 4.3 59.7 1.0
S A:SO4812 4.3 35.8 0.8
CA A:LEU373 4.4 49.4 1.0
O1 A:SO4812 4.4 36.0 0.8
O A:HOH902 4.6 25.0 1.0
OD2 A:ASP411 4.7 47.9 1.0
C A:ASP411 4.7 36.3 1.0
NE2 A:GLN524 4.8 54.2 1.0
C A:ILE371 4.8 42.5 1.0
CB A:LEU373 4.8 49.5 1.0
CB A:THR412 4.8 36.4 1.0
CA A:ASP411 4.8 36.7 1.0
CB A:ASP411 4.8 39.0 1.0
N A:VAL413 4.9 37.8 1.0

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.
ISSN: ESSN 1091-6490
PubMed: 35363566
DOI: 10.1073/PNAS.2107994119
Page generated: Thu Apr 6 18:09:52 2023

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