Magnesium in PDB 8fzv: The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Ala- Ala Linker Variant, Expressed with Sumo Tag

The structure of The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Ala- Ala Linker Variant, Expressed with Sumo Tag, PDB code: 8fzv was solved by M.J.Pedroza Romo, S.Soleimani, T.Doukov, A.Lebedev, J.D.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.39 / 3.29
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	162.557, 162.557, 56.877, 90, 90, 120
R / Rfree (%)	28.2 / 31.4

The binding sites of Magnesium atom in the The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Ala- Ala Linker Variant, Expressed with Sumo Tag (pdb code 8fzv). 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 The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Ala- Ala Linker Variant, Expressed with Sumo Tag, PDB code: 8fzv:

Magnesium binding site 1 out of 1 in the The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Ala- Ala Linker Variant, Expressed with Sumo Tag


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Ala- Ala Linker Variant, Expressed with Sumo Tag within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg300 b:132.1 occ:1.00 OG1 A:THR158 2.1 128.8 1.0 OG A:SER94 2.2 117.7 1.0 OG A:SER92 2.4 119.7 1.0 CB A:SER92 2.8 113.1 1.0 CB A:SER94 2.9 115.5 1.0 N A:SER94 3.2 105.2 1.0 CB A:THR158 3.4 131.2 1.0 N A:THR158 3.4 121.4 1.0 CA A:SER94 3.7 110.4 1.0 CA A:THR158 3.8 119.8 1.0 C A:GLU157 3.9 117.5 1.0 N A:GLY93 4.0 120.2 1.0 CA A:SER92 4.1 109.5 1.0 CA A:GLU157 4.1 117.4 1.0 O A:GLY156 4.2 134.1 1.0 C A:SER92 4.2 121.5 1.0 C A:GLY93 4.3 120.2 1.0 CG2 A:THR158 4.4 128.9 1.0 O A:GLU157 4.6 123.0 1.0 O A:LYS190 4.6 137.7 1.0 CA A:GLY93 4.7 120.3 1.0 OD2 A:ASP90 4.7 114.5 1.0 C A:SER94 4.9 112.8 1.0 OD1 A:ASP90 4.9 112.9 1.0

P.L.Gajjar, M.J.P.Romo, C.M.Litchfield, M.Callahan, N.Redd, S.Nawarathnage, S.Soleimani, J.Averett, E.Wilson, A.Lewis, C.Stewart, Y.J.Tseng, T.Doukov, A.Lebedev, J.D.Moody. Decreasing the Flexibility of the Telsam-Target Protein Linker and Omitting the Cleavable Fusion Tag Improves Crystal Order and Diffraction Limits. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 37293010
DOI: 10.1101/2023.05.12.540586