Magnesium in PDB 7ruv: Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin

All present enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin:
2.5.1.17;

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin, PDB code: 7ruv was solved by R.Mascarenhas, H.Gouda, M.Koutmos, R.Banerjee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.00 / 2.10
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	121.181, 121.181, 169.77, 90, 90, 120
R / Rfree (%)	18.5 / 21.7

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin also contains other interesting chemical elements:

Cobalt	(Co)	4 atoms
Potassium	(K)	1 atom

The binding sites of Magnesium atom in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin (pdb code 7ruv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin, PDB code: 7ruv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:45.5 occ:0.33 NZ A:LYS177 4.0 71.8 1.0 CZ A:PHE98 4.2 42.3 1.0 CD A:LYS177 4.3 61.5 1.0 CD2 A:LEU102 4.3 48.2 1.0 CE A:LYS177 4.8 65.9 1.0 CE1 A:PHE98 4.8 42.3 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg502 b:36.6 occ:1.00 NH1 C:ARG195 3.1 36.4 1.0 O C:HOH614 3.3 39.5 1.0 CD C:ARG191 3.9 37.8 1.0 CZ C:ARG195 4.3 45.4 1.0 NH2 C:ARG191 4.3 33.0 1.0 OE2 C:GLU84 4.4 47.3 1.0 NE C:ARG191 4.5 38.3 1.0 NE C:ARG195 4.6 42.0 1.0 CZ C:ARG191 4.7 39.9 1.0 CG C:ARG191 4.9 38.5 1.0

H.Gouda, R.Mascarenhas, S.Pillay, M.Ruetz, M.Koutmos, R.Banerjee. Patient Mutations in Human Atp:Cob(I)Alamin Adenosyltransferase Differentially Affect Its Catalytic Versus Chaperone Functions. J.Biol.Chem. 01373 2021.
ISSN: ESSN 1083-351X
PubMed: 34757128
DOI: 10.1016/J.JBC.2021.101373