Magnesium in PDB 6z1n: Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex

All present enzymatic activity of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex:
2.5.1.87;

The structure of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex, PDB code: 6z1n was solved by M.Lisnyansky Bar-El, Y.Haitin, M.Giladi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.98 / 2.30
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	184.074, 184.074, 112.593, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 22.3

The binding sites of Magnesium atom in the Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex (pdb code 6z1n). 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 Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex, PDB code: 6z1n:

Magnesium binding site 1 out of 1 in the Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Human Heterotetrameric Cis-Prenyltransferase Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:44.4 occ:1.00 O A:HOH507 2.0 44.9 1.0 O2B A:FPP401 2.0 42.6 1.0 OD1 A:ASP34 2.1 46.7 1.0 O A:HOH555 2.1 46.6 1.0 O A:HOH547 2.2 46.4 1.0 O2A A:FPP401 2.2 46.0 1.0 CG A:ASP34 3.0 47.0 1.0 PB A:FPP401 3.2 49.1 1.0 PA A:FPP401 3.3 44.7 1.0 OD2 A:ASP34 3.3 56.1 1.0 O3A A:FPP401 3.6 52.2 1.0 O1 A:FPP401 3.7 48.9 1.0 NH2 A:ARG38 3.7 46.5 1.0 O1B A:FPP401 3.8 48.4 1.0 O A:HOH566 3.9 47.7 1.0 C1 A:FPP401 4.2 48.4 1.0 N A:GLY35 4.2 36.7 1.0 O A:HOH538 4.3 40.0 1.0 NH2 A:ARG85 4.3 43.0 1.0 CB A:ASP34 4.4 40.1 1.0 O A:HOH512 4.4 67.1 1.0 O2 A:PO4402 4.4 69.0 1.0 O3B A:FPP401 4.5 52.5 1.0 O1A A:FPP401 4.6 49.9 1.0 CA A:ASP34 4.7 41.2 1.0 NH2 A:ARG205 4.8 41.2 1.0 CZ A:ARG38 4.9 53.4 1.0 NH2 A:ARG37 4.9 50.5 1.0 C A:ASP34 5.0 34.9 1.0

M.L.Bar-El, P.Vankova, A.Yeheskel, L.Simhaev, H.Engel, P.Man, Y.Haitin, M.Giladi. Structural Basis of Heterotetrameric Assembly and Disease Mutations in the Human Cis-Prenyltransferase Complex. Nat Commun V. 11 5273 2020.
ISSN: ESSN 2041-1723
PubMed: 33077723
DOI: 10.1038/S41467-020-18970-Z