Magnesium in PDB 5vrh: Apolipoprotein N-Acyltransferase C387S Active Site Mutant

The structure of Apolipoprotein N-Acyltransferase C387S Active Site Mutant, PDB code: 5vrh was solved by J.M.Murray, C.L.Noland, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.04 / 2.14
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.671, 72.586, 75.610, 90.00, 101.73, 90.00
R / Rfree (%)	20.7 / 25

The structure of Apolipoprotein N-Acyltransferase C387S Active Site Mutant also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Apolipoprotein N-Acyltransferase C387S Active Site Mutant (pdb code 5vrh). 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 Apolipoprotein N-Acyltransferase C387S Active Site Mutant, PDB code: 5vrh:

Magnesium binding site 1 out of 1 in the Apolipoprotein N-Acyltransferase C387S Active Site Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Apolipoprotein N-Acyltransferase C387S Active Site Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg603 b:31.9 occ:1.00 OE2 A:GLU381 2.1 59.0 1.0 OD2 A:ASP403 2.5 54.9 1.0 O A:HOH844 2.9 45.5 1.0 CD A:GLU381 2.9 57.4 1.0 OE1 A:GLU381 3.1 61.6 1.0 CG A:ASP403 3.1 52.9 1.0 CB A:ASP403 3.5 44.6 1.0 OD1 A:ASP403 4.0 57.6 1.0 O A:HOH825 4.1 35.8 1.0 CG A:GLU381 4.3 49.5 1.0 CA A:ASP403 4.9 35.8 1.0 O A:ASP403 4.9 30.0 1.0

C.L.Noland, M.D.Kattke, J.Diao, S.L.Gloor, H.Pantua, M.Reichelt, A.K.Katakam, D.Yan, J.Kang, I.Zilberleyb, M.Xu, S.B.Kapadia, J.M.Murray. Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase. Proc. Natl. Acad. Sci. V. 114 E6044 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28698362
DOI: 10.1073/PNAS.1707813114