Magnesium in PDB 5x0e: Free Serine Kinase (E30A Mutant) in Complex with Phosphoserine and Amp

The structure of Free Serine Kinase (E30A Mutant) in Complex with Phosphoserine and Amp, PDB code: 5x0e was solved by R.Nagata, M.Fujihashi, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	35.667, 43.224, 157.519, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 22.2

The binding sites of Magnesium atom in the Free Serine Kinase (E30A Mutant) in Complex with Phosphoserine and Amp (pdb code 5x0e). 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 Free Serine Kinase (E30A Mutant) in Complex with Phosphoserine and Amp, PDB code: 5x0e:

Magnesium binding site 1 out of 1 in the Free Serine Kinase (E30A Mutant) in Complex with Phosphoserine and Amp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Free Serine Kinase (E30A Mutant) in Complex with Phosphoserine and Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:9.6 occ:1.00 O1P A:SEP302 2.0 8.1 1.0 O3P A:AMP301 2.1 9.8 1.0 OD1 A:ASP69 2.1 9.0 1.0 O A:HOH469 2.1 7.8 1.0 O A:HOH455 2.2 6.3 1.0 O A:HOH416 2.2 6.7 1.0 CG A:ASP69 3.2 9.4 1.0 P A:AMP301 3.3 10.0 1.0 P A:SEP302 3.4 8.4 1.0 OD2 A:ASP69 3.6 9.6 1.0 O2P A:AMP301 3.7 9.9 1.0 O5' A:AMP301 3.8 10.1 1.0 O3P A:SEP302 3.9 8.4 1.0 OE2 A:GLU4 3.9 14.6 1.0 NZ A:LYS221 3.9 11.0 1.0 NH2 A:ARG73 3.9 9.9 1.0 O3' A:AMP301 4.1 10.6 1.0 CB A:SEP302 4.1 8.5 1.0 N A:GLY70 4.2 9.5 1.0 CA A:SEP302 4.2 8.5 1.0 OE1 A:GLU4 4.2 14.8 1.0 OG A:SEP302 4.3 8.5 1.0 O A:SEP302 4.3 8.8 1.0 O2P A:SEP302 4.5 8.3 1.0 CD A:GLU4 4.5 14.0 1.0 CB A:ASP69 4.5 9.2 1.0 O1P A:AMP301 4.5 9.4 1.0 C A:SEP302 4.6 8.8 1.0 C3' A:AMP301 4.7 11.2 1.0 C4' A:AMP301 4.7 10.9 1.0 C A:ASP69 4.8 9.4 1.0 CA A:ASP69 4.8 9.4 1.0 CA A:GLY70 4.9 9.7 1.0 C5' A:AMP301 4.9 10.8 1.0

R.Nagata, M.Fujihashi, H.Kawamura, T.Sato, T.Fujita, H.Atomi, K.Miki. Structural Study on the Reaction Mechanism of A Free Serine Kinase Involved in Cysteine Biosynthesis Acs Chem. Biol. V. 12 1514 2017.
ISSN: ESSN 1554-8937
PubMed: 28358477
DOI: 10.1021/ACSCHEMBIO.7B00064