Magnesium in PDB 2zi4: C4S Dck Variant of Dck in Complex with L-Da+Adp

All present enzymatic activity of C4S Dck Variant of Dck in Complex with L-Da+Adp:
2.7.1.74;

The structure of C4S Dck Variant of Dck in Complex with L-Da+Adp, PDB code: 2zi4 was solved by E.Sabini, A.Lavie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.10
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.730, 79.730, 93.530, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 25.7

The binding sites of Magnesium atom in the C4S Dck Variant of Dck in Complex with L-Da+Adp (pdb code 2zi4). 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 C4S Dck Variant of Dck in Complex with L-Da+Adp, PDB code: 2zi4:

Magnesium binding site 1 out of 1 in the C4S Dck Variant of Dck in Complex with L-Da+Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of C4S Dck Variant of Dck in Complex with L-Da+Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:27.7 occ:1.00 O A:HOH551 2.2 19.6 1.0 OG A:SER35 2.3 23.2 1.0 O1B A:ADP301 2.4 23.0 1.0 OE1 A:GLU127 2.4 26.5 1.0 O A:HOH537 2.8 41.6 1.0 CB A:SER35 3.4 23.1 1.0 CD A:GLU127 3.5 29.1 1.0 PB A:ADP301 3.5 22.1 1.0 N A:SER35 3.7 22.5 1.0 O3B A:ADP301 3.8 19.6 1.0 OE2 A:GLU127 3.9 31.4 1.0 CA A:SER35 4.0 23.3 1.0 O A:HOH530 4.1 35.2 1.0 O5' A:3L1401 4.2 25.2 1.0 O2B A:ADP301 4.4 21.3 1.0 O2A A:ADP301 4.5 19.6 1.0 O A:HOH504 4.5 22.9 1.0 NH2 A:ARG194 4.6 26.3 1.0 CB A:LYS34 4.6 21.3 1.0 O3A A:ADP301 4.7 19.9 1.0 C A:LYS34 4.7 22.2 1.0 CG A:GLU127 4.7 26.3 1.0 OE2 A:GLU53 4.8 29.4 1.0 O A:HOH503 4.8 14.8 1.0 NZ A:LYS34 4.9 17.9 1.0 PA A:ADP301 5.0 20.0 1.0

E.Sabini, S.Hazra, S.Ort, M.Konrad, A.Lavie. Structural Basis For Substrate Promiscuity of Dck J.Mol.Biol. V. 378 607 2008.
ISSN: ISSN 0022-2836
PubMed: 18377927
DOI: 10.1016/J.JMB.2008.02.061