Magnesium in PDB 3u6k: Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733

The structure of Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733, PDB code: 3u6k was solved by D.J.Palestrant, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.04 / 2.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	80.372, 82.216, 129.900, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733 (pdb code 3u6k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733, PDB code: 3u6k:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg394 b:41.9 occ:1.00 O A:HOH444 2.2 43.1 1.0 OG1 A:THR25 2.2 49.2 1.0 O A:HOH439 2.3 37.1 1.0 O3B A:GDP500 2.5 51.9 1.0 O A:HOH442 2.6 47.6 1.0 O A:HOH441 2.7 42.1 1.0 O1B A:GDP500 3.5 56.7 1.0 CB A:THR25 3.6 48.9 1.0 PB A:GDP500 3.6 56.2 1.0 O A:CYS81 3.7 49.2 1.0 O A:HOH443 3.9 29.9 1.0 CA A:PRO82 4.0 49.7 1.0 OD1 A:ASP50 4.1 65.9 1.0 O A:PRO82 4.2 50.8 1.0 CG2 A:THR25 4.4 48.6 1.0 OD2 A:ASP80 4.4 51.1 1.0 C A:CYS81 4.4 49.7 1.0 O2A A:GDP500 4.5 65.0 1.0 N A:THR25 4.6 48.5 1.0 O3A A:GDP500 4.6 60.1 1.0 C A:PRO82 4.6 50.1 1.0 CA A:THR25 4.6 49.1 1.0 N A:PRO82 4.6 49.4 1.0 O2B A:GDP500 4.8 55.4 1.0 OD1 A:ASP80 4.8 47.1 1.0 CB A:PRO82 4.8 48.7 1.0

Magnesium binding site 2 out of 2 in the Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Ef-Tu (Escherichia Coli) in Complex with Nvp-LDK733 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg394 b:46.5 occ:1.00 O B:HOH395 2.2 48.1 1.0 O B:HOH403 2.3 38.4 1.0 O B:HOH396 2.3 29.5 1.0 O B:HOH397 2.4 48.4 1.0 O3B B:GDP500 2.4 41.8 1.0 OG1 B:THR25 2.4 47.3 1.0 O1B B:GDP500 3.3 45.2 1.0 PB B:GDP500 3.4 43.2 1.0 CB B:THR25 3.6 47.0 1.0 OD1 B:ASP50 3.9 76.8 1.0 CA B:PRO82 4.2 51.6 1.0 O B:CYS81 4.2 51.6 1.0 OD2 B:ASP80 4.3 49.5 1.0 O B:PRO82 4.4 55.6 1.0 O2A B:GDP500 4.4 47.3 1.0 O3A B:GDP500 4.4 45.7 1.0 CG2 B:THR25 4.4 44.2 1.0 O2B B:GDP500 4.5 39.8 1.0 N B:THR25 4.6 42.8 1.0 C B:PRO82 4.6 53.1 1.0 CA B:THR25 4.7 45.5 1.0 CE B:LYS24 4.7 36.8 1.0 OD1 B:ASP80 4.8 49.6 1.0 C B:CYS81 4.9 50.5 1.0 PA B:GDP500 4.9 48.9 1.0 N B:PRO82 4.9 51.1 1.0 CG B:ASP80 5.0 48.9 1.0

M.J.Lamarche, J.A.Leeds, K.Amaral, J.T.Brewer, S.M.Bushell, J.M.Dewhurst, J.Dzink-Fox, E.Gangl, J.Goldovitz, A.Jain, S.Mullin, G.Neckermann, C.Osborne, D.Palestrant, M.A.Patane, E.M.Rann, M.Sachdeva, J.Shao, S.Tiamfook, L.Whitehead, D.Yu. Antibacterial Optimization of 4-Aminothiazolyl Analogues of the Natural Product GE2270 A: Identification of the Cycloalkylcarboxylic Acids. J.Med.Chem. V. 54 8099 2011.
ISSN: ISSN 0022-2623
PubMed: 21999529
DOI: 10.1021/JM200938F