Magnesium in PDB 3gu7: Crystal Structure of DAPKQ23V-Adp-MG2+

All present enzymatic activity of Crystal Structure of DAPKQ23V-Adp-MG2+:
2.7.11.1;

The structure of Crystal Structure of DAPKQ23V-Adp-MG2+, PDB code: 3gu7 was solved by L.K.Mcnamara, J.S.Schavocky, D.M.Watterson, J.S.Brunzelle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.56 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.861, 62.365, 88.262, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 22.8

The binding sites of Magnesium atom in the Crystal Structure of DAPKQ23V-Adp-MG2+ (pdb code 3gu7). 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 DAPKQ23V-Adp-MG2+, PDB code: 3gu7:

Magnesium binding site 1 out of 1 in the Crystal Structure of DAPKQ23V-Adp-MG2+


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 DAPKQ23V-Adp-MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg297 b:37.9 occ:1.00 O A:HOH517 1.7 26.3 1.0 OD2 A:ASP161 2.2 16.6 1.0 O1A A:ADP296 2.2 25.2 1.0 O3B A:ADP296 2.3 35.8 1.0 O A:HOH490 2.5 38.5 1.0 O A:HOH385 2.5 32.1 1.0 ND2 A:ASN144 3.0 14.5 1.0 CG A:ASP161 3.1 16.8 1.0 PA A:ADP296 3.3 24.3 1.0 PB A:ADP296 3.5 35.9 1.0 O3A A:ADP296 3.7 29.2 1.0 CB A:ASP161 3.7 15.2 1.0 OD1 A:ASN144 3.8 17.3 1.0 OE2 A:GLU143 3.8 31.0 1.0 CG A:ASN144 3.8 15.7 1.0 O1B A:ADP296 4.0 37.0 1.0 OD1 A:ASP161 4.0 15.1 1.0 O3' A:ADP296 4.2 24.5 1.0 O A:HOH437 4.3 44.9 1.0 C5' A:ADP296 4.4 23.6 1.0 O5' A:ADP296 4.4 24.6 1.0 OD2 A:ASP139 4.4 22.1 1.0 O2A A:ADP296 4.4 21.7 1.0 CD A:GLU143 4.5 29.3 1.0 CG A:GLU143 4.7 27.6 1.0 C3' A:ADP296 4.7 24.3 1.0 O2B A:ADP296 4.8 34.6 1.0 O A:HOH513 4.8 27.2 1.0

L.K.Mcnamara, J.S.Schavocky, D.M.Watterson, J.S.Brunzelle. Enzyme Activity and Crystallographic Analyses of A Glycine-Rich Loop Mutant of Dapk To Be Published.