Magnesium in PDB 8a6u: PCIDS1 in Complex with MG2+

All present enzymatic activity of PCIDS1 in Complex with MG2+:
2.5.1.1;

The structure of PCIDS1 in Complex with MG2+, PDB code: 8a6u was solved by F.Ecker, W.Boland, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.16, 78.33, 89.61, 90, 101.71, 90
R / Rfree (%)	15.5 / 19.5

The binding sites of Magnesium atom in the PCIDS1 in Complex with MG2+ (pdb code 8a6u). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the PCIDS1 in Complex with MG2+, PDB code: 8a6u:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the PCIDS1 in Complex with MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of PCIDS1 in Complex with MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:41.2 occ:1.00 O A:HOH653 2.1 32.3 1.0 O A:HOH752 2.1 45.4 1.0 O A:HOH623 2.1 40.9 1.0 OD2 A:ASP319 2.1 35.9 1.0 O A:HOH683 2.1 38.3 1.0 O A:HOH702 2.1 36.9 1.0 CG A:ASP319 3.2 34.0 1.0 OD1 A:ASP319 3.7 39.5 1.0 OD1 A:ASP323 4.0 37.3 1.0 OD2 A:ASP337 4.2 36.0 1.0 NE2 A:GLN316 4.2 33.9 1.0 OD1 A:ASP337 4.2 36.2 1.0 CB A:ASP319 4.4 30.7 1.0 O A:HOH708 4.4 48.6 1.0 O A:ASP319 4.5 34.6 1.0 OD1 A:ASP320 4.6 30.7 1.0 O A:HOH789 4.6 69.2 1.0 CG A:ASP337 4.7 35.8 1.0 C A:ASP319 4.7 32.6 1.0 CG A:ASP323 4.7 35.4 1.0 O A:HOH607 4.8 54.1 1.0 O A:HOH776 4.8 70.7 1.0 CB A:ASP323 4.9 33.6 1.0 O A:HOH617 4.9 57.2 1.0

Magnesium binding site 2 out of 2 in the PCIDS1 in Complex with MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of PCIDS1 in Complex with MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:34.0 occ:1.00 O B:HOH667 2.0 35.4 1.0 OD2 B:ASP319 2.1 33.1 1.0 O B:HOH835 2.1 37.8 1.0 O B:HOH697 2.1 35.1 1.0 O B:HOH777 2.1 37.5 1.0 O B:HOH612 2.2 28.6 1.0 CG B:ASP319 3.2 31.4 1.0 OD1 B:ASP319 3.6 34.8 1.0 OD1 B:ASP323 4.0 32.4 1.0 NE2 B:GLN316 4.2 28.0 1.0 OD2 B:ASP337 4.2 30.9 1.0 OD1 B:ASP337 4.3 31.0 1.0 CB B:ASP319 4.4 29.3 1.0 O B:ASP319 4.4 27.5 1.0 O B:HOH712 4.4 39.6 1.0 OD1 B:ASP320 4.5 28.3 1.0 O B:HOH847 4.6 64.6 1.0 C B:ASP319 4.7 25.9 1.0 CG B:ASP337 4.7 31.2 1.0 CG B:ASP323 4.8 31.0 1.0 O B:HOH634 4.8 61.1 1.0 CB B:ASP323 4.9 30.8 1.0

F.Ecker, W.Boland, M.Groll. Metal-Dependent Enzyme Symmetry Guides the Biosynthetic Flux of Terpene Precursors To Be Published 2023.
DOI: 10.1038/S41557-023-01235-9