Magnesium in PDB 6mfw: Crystal Structure of A 4-Domain Construct of Lgra in the Substrate Donation State

The structure of Crystal Structure of A 4-Domain Construct of Lgra in the Substrate Donation State, PDB code: 6mfw was solved by J.M.Reimer, M.Eivaskhani, T.M.Schmeing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	69.33 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.370, 133.870, 162.099, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.4

The binding sites of Magnesium atom in the Crystal Structure of A 4-Domain Construct of Lgra in the Substrate Donation State (pdb code 6mfw). 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 A 4-Domain Construct of Lgra in the Substrate Donation State, PDB code: 6mfw:

Magnesium binding site 1 out of 1 in the Crystal Structure of A 4-Domain Construct of Lgra in the Substrate Donation State


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 A 4-Domain Construct of Lgra in the Substrate Donation State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1306 b:36.2 occ:1.00 O A:HOH1532 1.9 54.7 1.0 O2G A:APC1303 2.0 67.5 1.0 O A:HOH1484 2.2 49.9 1.0 O1B A:APC1303 2.6 53.4 1.0 O A:HOH1420 2.9 50.4 1.0 PG A:APC1303 3.3 65.5 1.0 H3A2 A:APC1303 3.4 61.9 1.0 PB A:APC1303 3.5 55.4 1.0 O3B A:APC1303 3.6 60.5 1.0 C3A A:APC1303 3.9 51.5 1.0 O3G A:APC1303 4.0 61.0 1.0 HG21 A:THR351 4.1 64.2 1.0 OE2 A:GLU485 4.1 39.8 1.0 O A:HOH1497 4.2 45.1 1.0 HB A:THR351 4.3 65.8 1.0 HG22 A:THR351 4.3 64.2 1.0 OE1 A:GLU485 4.4 39.4 1.0 O1G A:APC1303 4.4 60.7 1.0 O2A A:APC1303 4.5 51.5 1.0 CG2 A:THR351 4.6 53.4 1.0 HZ1 A:LYS359 4.7 82.1 1.0 H3A1 A:APC1303 4.7 61.9 1.0 CD A:GLU485 4.7 40.2 1.0 HH A:TYR564 4.8 48.9 1.0 O2B A:APC1303 4.9 62.1 1.0 PA A:APC1303 4.9 43.5 1.0 HZ2 A:LYS359 4.9 82.1 1.0 CB A:THR351 4.9 54.8 1.0

J.M.Reimer, M.Eivaskhani, I.Harb, A.Guarne, M.Weigt, T.M.Schmeing. Structures of A Dimodular Nonribosomal Peptide Synthetase Reveal Conformational Flexibility. Science V. 366 2019.
ISSN: ESSN 1095-9203
PubMed: 31699907
DOI: 10.1126/SCIENCE.AAW4388