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Magnesium in PDB 7zvm: Thermococcus Barophilus Phosphomannose Isomerase Protein Structure at 1.6 A

Protein crystallography data

The structure of Thermococcus Barophilus Phosphomannose Isomerase Protein Structure at 1.6 A, PDB code: 7zvm was solved by F.Hoh, A.Calio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.58 / 1.58
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 48.482, 52.41, 112.868, 90, 90, 90
R / Rfree (%) 17.4 / 21.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Thermococcus Barophilus Phosphomannose Isomerase Protein Structure at 1.6 A (pdb code 7zvm). 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 Thermococcus Barophilus Phosphomannose Isomerase Protein Structure at 1.6 A, PDB code: 7zvm:

Magnesium binding site 1 out of 1 in 7zvm

Go back to Magnesium Binding Sites List in 7zvm
Magnesium binding site 1 out of 1 in the Thermococcus Barophilus Phosphomannose Isomerase Protein Structure at 1.6 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Thermococcus Barophilus Phosphomannose Isomerase Protein Structure at 1.6 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:47.2
occ:1.00
NE2 A:HIS85 2.1 25.6 1.0
OE1 A:GLU51 2.2 49.2 1.0
NE2 A:HIS46 2.4 27.4 1.0
CE1 A:HIS85 3.1 22.6 1.0
NE2 A:HIS44 3.1 20.9 1.0
CD A:GLU51 3.2 30.2 1.0
CD2 A:HIS85 3.2 23.8 1.0
CD2 A:HIS46 3.3 24.7 1.0
CE1 A:HIS46 3.3 29.5 1.0
OE2 A:GLU51 3.7 41.8 1.0
CD2 A:HIS44 3.9 23.4 1.0
CE1 A:HIS44 4.0 21.9 1.0
ND1 A:HIS85 4.2 22.9 1.0
CG A:HIS85 4.3 21.9 1.0
CG A:GLU51 4.4 31.0 1.0
CZ A:PHE53 4.5 30.4 1.0
ND1 A:HIS46 4.5 28.5 1.0
CG A:HIS46 4.5 22.8 1.0

Reference:

A.Calio, C.Dubois, S.Fontanay, M.M.Koza, F.Hoh, C.Roumestand, P.Oger, J.Peters. Unravelling the Adaptation Mechanisms to High Pressure in Proteins. Int J Mol Sci V. 23 2022.
ISSN: ESSN 1422-0067
PubMed: 35955607
DOI: 10.3390/IJMS23158469
Page generated: Thu Oct 3 17:05:57 2024

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