Potassium in PDB 8fzu: The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val 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, Thr- Val Linker Variant, Expressed with Sumo Tag, PDB code: 8fzu was solved by P.L.Gajjar, C.M.Litchfield, M.Callahan, N.Redd, 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)	71.06 / 1.90
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	164.096, 164.096, 54.401, 90, 90, 120
R / Rfree (%)	23.8 / 26.6

The binding sites of Potassium atom in the The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Expressed with Sumo Tag (pdb code 8fzu). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Expressed with Sumo Tag, PDB code: 8fzu:

Potassium 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, Thr- Val Linker Variant, Expressed with Sumo Tag


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Expressed with Sumo Tag within 5.0Å range: probe atom residue distance (Å) B Occ B:K301 b:44.8 occ:1.00 O B:ILE14 2.6 20.8 1.0 CE B:LYS47 2.9 35.9 1.0 O B:HOH731 3.1 29.6 1.0 O B:HOH533 3.1 23.7 1.0 CG B:LYS47 3.5 28.3 1.0 O B:HOH669 3.5 25.8 1.0 CD B:LYS47 3.5 29.7 1.0 C B:ILE14 3.6 21.8 1.0 NZ B:LYS47 3.6 41.8 1.0 CG1 B:ILE14 3.8 20.0 1.0 CD1 B:TYR15 3.8 23.6 1.0 O B:HOH535 4.0 13.9 1.0 CA B:TYR15 4.1 19.0 1.0 N B:TYR15 4.2 22.3 1.0 O B:HOH554 4.2 33.0 1.0 CE1 B:TYR15 4.3 19.8 1.0 CD1 B:ILE14 4.5 24.8 1.0 CA B:ILE14 4.6 21.9 1.0 CB B:ILE14 4.6 16.8 1.0 CG B:TYR15 4.6 20.2 1.0 CG2 B:ILE14 4.8 17.2 1.0 CB B:TYR15 4.9 18.2 1.0 CB B:LYS47 4.9 22.9 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