Magnesium in PDB 4wmu: Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A

The structure of Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A, PDB code: 4wmu was solved by M.C.Clifton, J.W.Faiman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.46 / 1.55
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	98.870, 135.900, 37.680, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 19

The structure of Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A (pdb code 4wmu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A, PDB code: 4wmu:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:10.2 occ:0.54 OD1 A:ASP167 2.0 17.4 1.0 O A:HOH526 2.1 21.2 1.0 O2 A:FMT406 2.1 21.5 1.0 O A:HOH577 2.1 21.6 1.0 O A:HOH565 2.1 19.1 1.0 C A:FMT406 3.0 20.4 1.0 CG A:ASP167 3.0 16.4 1.0 OD2 A:ASP167 3.4 21.3 1.0 O1 A:FMT406 4.2 20.2 1.0 OE1 A:GLU163 4.2 20.0 1.0 O A:HOH617 4.3 34.5 1.0 CB A:ASP167 4.3 14.0 1.0 O A:GLU163 4.4 15.0 1.0 O A:VAL307 4.5 15.8 1.0 CA A:ASP167 4.6 12.7 1.0 CG A:ARG310 4.6 23.0 1.0 N A:ASP167 4.6 11.8 1.0 CG A:LYS166 4.7 22.2 1.0

Magnesium binding site 2 out of 2 in the Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:56.9 occ:1.00 O A:HOH503 2.1 36.8 1.0 O A:HOH549 2.2 32.1 1.0 O A:HOH1004 2.3 49.2 1.0 O A:HOH587 2.3 43.0 1.0 O A:HOH955 3.9 36.9 1.0 OG A:SER202 4.0 38.6 1.0 O A:HOH956 4.0 36.3 1.0 O A:HOH1005 4.0 40.2 1.0 O A:HOH640 4.1 32.4 1.0 OE2 A:GLU173 4.3 19.3 0.6 OG1 A:THR205 4.6 26.2 1.0 OE2 A:GLU173 4.6 26.0 0.4 OE1 A:GLU173 4.6 21.0 0.4 CB A:SER202 4.7 31.8 1.0 OD2 A:ASP313 4.8 29.6 1.0

M.C.Clifton, D.M.Dranow, A.Leed, B.Fulroth, J.W.Fairman, J.Abendroth, K.A.Atkins, E.Wallace, D.Fan, G.Xu, Z.J.Ni, D.Daniels, J.Van Drie, G.Wei, A.B.Burgin, T.R.Golub, B.K.Hubbard, M.H.Serrano-Wu. A Maltose-Binding Protein Fusion Construct Yields A Robust Crystallography Platform For MCL1. Plos One V. 10 25010 2015.
ISSN: ESSN 1932-6203
PubMed: 25909780
DOI: 10.1371/JOURNAL.PONE.0125010