Magnesium in PDB 4mzf: Crystal Structure of Human SPINDLIN1 Bound to Histone H3(K4ME3-R8ME2A) Peptide

The structure of Crystal Structure of Human SPINDLIN1 Bound to Histone H3(K4ME3-R8ME2A) Peptide, PDB code: 4mzf was solved by X.Su, X.Ding, H.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.78 / 2.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	120.679, 43.309, 50.150, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 25.5

The structure of Crystal Structure of Human SPINDLIN1 Bound to Histone H3(K4ME3-R8ME2A) Peptide also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human SPINDLIN1 Bound to Histone H3(K4ME3-R8ME2A) Peptide (pdb code 4mzf). 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 Crystal Structure of Human SPINDLIN1 Bound to Histone H3(K4ME3-R8ME2A) Peptide, PDB code: 4mzf:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human SPINDLIN1 Bound to Histone H3(K4ME3-R8ME2A) Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human SPINDLIN1 Bound to Histone H3(K4ME3-R8ME2A) Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg303 b:26.7 occ:0.50 O B:HOH463 2.1 25.7 1.0 O B:HOH447 2.1 26.0 1.0 O B:HOH464 2.2 35.4 1.0 OE2 B:GLU138 4.0 30.5 1.0 O B:GLU150 4.0 31.4 1.0 OE1 B:GLU138 4.2 33.5 1.0 OE2 B:GLU150 4.4 38.5 1.0 CD B:GLU138 4.5 33.5 1.0 CL B:CL301 4.5 28.3 1.0 NH2 B:ARG152 4.7 40.1 1.0 C B:GLU150 4.9 28.5 1.0 CB B:GLU150 4.9 34.6 1.0 CG B:GLU150 5.0 33.1 1.0

X.Su, G.Zhu, X.Ding, S.Y.Lee, Y.Dou, B.Zhu, W.Wu, H.Li. Molecular Basis Underlying Histone H3 Lysine-Arginine Methylation Pattern Readout By Spin/Ssty Repeats of SPINDLIN1 Genes Dev. V. 28 622 2014.
ISSN: ISSN 0890-9369
PubMed: 24589551
DOI: 10.1101/GAD.233239.113