Magnesium in PDB 8ihy: X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida

The structure of X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida, PDB code: 8ihy was solved by C.Kuroki, Y.Hirano, M.Nakazawa, T.Sakamoto, T.Tamada, M.Ueda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.29 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.36, 71.639, 55.184, 90, 114.04, 90
R / Rfree (%)	14.7 / 17.7

The structure of X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida (pdb code 8ihy). 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 X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida, PDB code: 8ihy:

Magnesium binding site 1 out of 1 in the X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:13.4 occ:1.00 O A:HOH856 2.0 12.3 1.0 O A:HOH833 2.1 16.3 1.0 OE1 A:GLN404 2.1 9.9 1.0 O A:HOH606 2.1 16.7 1.0 OD1 A:ASP386 2.2 12.9 1.0 CD A:GLN404 3.1 6.4 1.0 CG A:ASP386 3.1 15.4 1.0 OD2 A:ASP386 3.3 12.8 1.0 NE2 A:GLN404 3.3 9.0 1.0 O A:HOH995 4.0 20.7 1.0 O A:HOH954 4.2 17.4 1.0 O A:TYR403 4.4 8.1 1.0 O A:HOH863 4.4 13.4 1.0 CG A:GLN404 4.4 6.3 1.0 CB A:ASP386 4.5 14.8 1.0 CB A:GLN404 4.8 7.2 1.0 CA A:GLN404 4.8 5.1 1.0 N A:ASP386 4.9 10.3 1.0 CA A:ASP386 4.9 9.5 1.0 C A:TYR403 5.0 6.9 1.0

C.Kuroki, Y.Hirano, M.Nakazawa, T.Sakamoto, T.Tamada, M.Ueda. A Single Mutation ASP43ARG Was Increased 2.5-Fold the Catalytic Activity and Maintained the Stability of Cold-Adapted Endo-1,4-Beta Glucanase (Ef-EG2) From Eisenia Fetida. Curr Res Biotechnol V. 5 2023.
DOI: 10.1016/J.CRBIOT.2023.100126