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Magnesium in PDB 7o6t: Crystal Structure of the Polymerising Vel Domain of VIN3 (R556D I575D Mutant)

Protein crystallography data

The structure of Crystal Structure of the Polymerising Vel Domain of VIN3 (R556D I575D Mutant), PDB code: 7o6t was solved by M.Fiedler, E.Franco-Echevarria, C.Dean, M.Bienz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.49 / 2.02
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 31.423, 51.809, 85.01, 90, 90, 90
R / Rfree (%) 20.2 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Polymerising Vel Domain of VIN3 (R556D I575D Mutant) (pdb code 7o6t). 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 Crystal Structure of the Polymerising Vel Domain of VIN3 (R556D I575D Mutant), PDB code: 7o6t:

Magnesium binding site 1 out of 1 in 7o6t

Go back to Magnesium Binding Sites List in 7o6t
Magnesium binding site 1 out of 1 in the Crystal Structure of the Polymerising Vel Domain of VIN3 (R556D I575D Mutant)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Polymerising Vel Domain of VIN3 (R556D I575D Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg701

b:52.8
occ:1.00
O B:HOH819 2.0 67.8 1.0
NE2 B:HIS535 2.5 78.0 1.0
OE1 A:GLU546 2.8 46.1 1.0
CD2 B:HIS535 3.3 76.3 1.0
CE1 B:HIS535 3.3 75.5 1.0
O A:HOH722 3.7 57.3 1.0
CD A:GLU546 4.0 49.0 1.0
ND1 B:HIS535 4.4 80.5 1.0
CG B:HIS535 4.4 69.9 1.0
OE2 A:GLU546 4.5 53.1 1.0
O A:GLU546 4.6 47.4 1.0
NZ B:LYS538 4.9 86.9 1.0

Reference:

M.Fiedler, E.Franco-Echevarria, A.Schulten, M.Nielsen, T.J.Rutherford, A.Yeates, B.Ahsan, C.Dean, M.Bienz. Head-to-Tail Polymerization By Vel Proteins Underpins Cold-Induced Polycomb Silencing in Flowering Control. Cell Rep V. 41 11607 2022.
ISSN: ESSN 2211-1247
PubMed: 36351412
DOI: 10.1016/J.CELREP.2022.111607
Page generated: Thu Apr 6 18:05:02 2023

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