Magnesium in PDB 7y43: Crystal Structure of the KAT6A Wh Domain and Its Bound Double Stranded Dna

All present enzymatic activity of Crystal Structure of the KAT6A Wh Domain and Its Bound Double Stranded Dna:
2.3.1.48;

The structure of Crystal Structure of the KAT6A Wh Domain and Its Bound Double Stranded Dna, PDB code: 7y43 was solved by Z.Wang, Y.Jia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.60 / 1.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	46.479, 46.479, 153.518, 90, 90, 90
R / Rfree (%)	22.7 / 23.5

The binding sites of Magnesium atom in the Crystal Structure of the KAT6A Wh Domain and Its Bound Double Stranded Dna (pdb code 7y43). 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 KAT6A Wh Domain and Its Bound Double Stranded Dna, PDB code: 7y43:

Magnesium binding site 1 out of 1 in the Crystal Structure of the KAT6A Wh Domain and Its Bound Double Stranded Dna


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 KAT6A Wh Domain and Its Bound Double Stranded Dna within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg101 b:38.9 occ:1.00 O A:HOH287 2.0 36.2 1.0 OD2 A:ASP75 2.0 39.9 1.0 O A:HOH234 2.2 22.3 1.0 O A:HOH230 2.3 42.9 1.0 O A:HOH218 2.5 37.5 1.0 CG A:ASP75 3.1 34.1 1.0 OD1 A:ASP75 3.6 36.3 1.0 OD1 A:ASP73 4.1 19.4 1.0 O A:HOH203 4.3 40.5 1.0 CB A:ASP75 4.3 25.1 1.0 O A:HOH201 4.3 34.3 1.0 OD2 A:ASP73 4.3 24.2 1.0 CG A:ASP73 4.7 20.6 1.0 CD1 A:LEU14 4.9 19.8 1.0

L.M.Weber, Y.Jia, B.Stielow, S.S.Gisselbrecht, Y.Cao, Y.Ren, I.Rohner, J.King, E.Rothman, S.Fischer, C.Simon, I.Forne, A.Nist, T.Stiewe, M.L.Bulyk, Z.Wang, R.Liefke. The Histone Acetyltransferase KAT6A Is Recruited to Unmethylated Cpg Islands Via A Dna Binding Winged Helix Domain Nucleic Acids Res. 2022.
ISSN: ESSN 1362-4962
DOI: 10.1093/NAR/GKAC1188