Magnesium in PDB 8fun: Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2

The structure of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2, PDB code: 8fun was solved by M.M.Powell, J.Rittle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.56 / 2.24
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	84.142, 148.923, 234.093, 90, 90, 90
R / Rfree (%)	17.7 / 19.8

The structure of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 also contains other interesting chemical elements:

Manganese	(Mn)	5 atoms
Iron	(Fe)	1 atom

The binding sites of Magnesium atom in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 (pdb code 8fun). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2, PDB code: 8fun:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:36.5 occ:0.50 O B:PRO290 2.4 23.9 1.0 O B:HOH714 2.8 26.4 1.0 C B:PRO290 3.5 23.6 1.0 CA B:PRO290 4.2 20.1 1.0 CB B:PRO290 4.4 25.0 1.0 N B:ASP291 4.6 22.7 1.0 CA B:ASP291 4.7 22.2 1.0

Magnesium binding site 2 out of 2 in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg402 b:35.8 occ:1.00 OD2 C:ASP327 2.2 26.7 1.0 O C:HOH593 2.4 30.0 1.0 O D:HOH513 2.9 35.4 1.0 CG C:ASP327 3.1 29.3 1.0 CB C:ASP327 3.2 27.5 1.0 NE2 D:HIS319 3.6 31.4 1.0 CA C:SER324 4.0 23.3 1.0 O C:SER324 4.2 27.3 1.0 CD2 D:HIS319 4.2 35.7 1.0 OD1 C:ASP327 4.3 23.7 1.0 CB C:SER324 4.5 26.5 1.0 OG C:SER324 4.6 33.1 1.0 C C:SER324 4.6 28.8 1.0 OE2 D:GLU322 4.6 31.1 1.0 CE1 D:HIS319 4.7 29.2 1.0 CA C:ASP327 4.7 24.3 1.0 O C:ASP323 4.7 27.1 1.0 N C:SER324 5.0 26.2 1.0 OE1 D:GLU322 5.0 31.4 1.0

M.M.Powell, G.Rao, R.D.Britt, J.Rittle. Enzymatic Hydroxylation of Aliphatic C-H Bonds By A Mn/Fe Cofactor. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 36945426
DOI: 10.1101/2023.03.10.532131