Magnesium in PDB 4ols: The Amidase-2 Domain of LYSGH15

The structure of The Amidase-2 Domain of LYSGH15, PDB code: 4ols was solved by J.Gu, S.Ouyang, Z.J.Liu, W.Han, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.57 / 2.27
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	135.400, 135.400, 107.077, 90.00, 90.00, 120.00
R / Rfree (%)	15.8 / 16.1

The structure of The Amidase-2 Domain of LYSGH15 also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Zinc	(Zn)	17 atoms

The binding sites of Magnesium atom in the The Amidase-2 Domain of LYSGH15 (pdb code 4ols). 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 Amidase-2 Domain of LYSGH15, PDB code: 4ols:

Magnesium binding site 1 out of 1 in the The Amidase-2 Domain of LYSGH15


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Amidase-2 Domain of LYSGH15 within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg504 b:18.1 occ:0.91 O D:HOH765 2.8 24.3 1.0 N D:GLY266 3.1 28.8 1.0 ND2 D:ASN275 3.2 26.6 1.0 CA D:GLY266 3.2 30.2 1.0 C D:TRP263 3.6 24.9 1.0 CB D:TRP263 3.7 20.0 1.0 CA D:TRP263 3.7 19.9 1.0 O D:HOH718 3.7 56.7 1.0 N D:HIS264 3.8 23.8 1.0 CG D:ASN275 4.0 25.8 1.0 OD1 D:ASN275 4.0 27.1 1.0 O D:TRP263 4.0 27.4 1.0 C D:GLY266 4.2 30.8 1.0 N D:THR265 4.2 21.7 1.0 C D:THR265 4.4 25.3 1.0 CG D:TRP263 4.5 25.9 1.0 C D:HIS264 4.5 22.3 1.0 N D:ASP267 4.6 27.9 1.0 ZN D:ZN501 4.6 0.9 1.0 CA D:HIS264 4.6 19.5 1.0 O A:HOH716 4.8 50.0 1.0 CD1 D:TRP263 4.8 30.0 1.0 CA D:THR265 4.9 23.9 1.0

J.Gu, F.Feng, X.Feng, C.Sun, L.Lei, W.Ding, F.Niu, L.Jiao, M.Yang, Y.Li, X.Liu, J.Song, Z.Cui, D.Han, C.Du, Y.Yang, S.Ouyang, Z.Liu, W.Han. Structural and Biochemical Characterization Reveals LYSGH15 As An Unprecedented "Ef-Hand-Like" Calcium-Binding Phage Lysin Plos Pathog. V. 10 04109 2014.
ISSN: ISSN 1553-7366
DOI: 10.1371/JOURNAL.PPAT.1004109