Magnesium in PDB 7cas: Versatile Cis-Prenyltransferase MM_0014 From Methanosarcina Mazei (Crystal Type: Free+Ppi)

The structure of Versatile Cis-Prenyltransferase MM_0014 From Methanosarcina Mazei (Crystal Type: Free+Ppi), PDB code: 7cas was solved by H.Unno, H.Hemmi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	65.04 / 2.28
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	79.779, 100.219, 130.09, 90, 90, 90
R / Rfree (%)	22 / 25.8

The binding sites of Magnesium atom in the Versatile Cis-Prenyltransferase MM_0014 From Methanosarcina Mazei (Crystal Type: Free+Ppi) (pdb code 7cas). 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 Versatile Cis-Prenyltransferase MM_0014 From Methanosarcina Mazei (Crystal Type: Free+Ppi), PDB code: 7cas:

Magnesium binding site 1 out of 1 in the Versatile Cis-Prenyltransferase MM_0014 From Methanosarcina Mazei (Crystal Type: Free+Ppi)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Versatile Cis-Prenyltransferase MM_0014 From Methanosarcina Mazei (Crystal Type: Free+Ppi) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:41.0 occ:1.00 O A:HOH403 1.8 60.7 1.0 O A:HOH408 1.9 59.6 1.0 O2 A:DPO302 1.9 46.6 1.0 O5 A:DPO302 1.9 41.3 1.0 OD1 A:ASP18 2.1 45.0 1.0 CG A:ASP18 2.8 44.6 1.0 OD2 A:ASP18 2.9 47.8 1.0 P2 A:DPO302 3.0 39.1 1.0 P1 A:DPO302 3.1 49.5 1.0 O7 A:DPO302 3.3 40.2 1.0 O4 A:DPO302 3.3 43.8 1.0 O1 A:DPO302 3.9 43.2 1.0 NH2 A:ARG69 4.2 85.2 1.0 CB A:ASP18 4.2 43.3 1.0 NH2 A:ARG21 4.2 49.5 1.0 O6 A:DPO302 4.3 40.1 1.0 NH1 A:ARG22 4.3 52.1 1.0 O3 A:DPO302 4.3 50.8 1.0 N A:GLY19 4.5 42.2 1.0 O A:HOH438 4.6 53.2 1.0 NH1 A:ARG69 4.7 85.7 1.0 CA A:ASP18 4.7 40.9 1.0 CZ A:ARG69 4.8 85.1 1.0 NH2 A:ARG168 4.9 36.8 1.0

M.Okada, H.Unno, K.Emi, M.Matsumoto, H.Hemmi. A Versatile Cis-Prenyltransferase From Methanosarcina Mazei Catalyzes Both C- and O-Prenylations. J.Biol.Chem. 2021.
ISSN: ESSN 1083-351X