Magnesium in PDB 8cbk: Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-His(5,Ser)

All present enzymatic activity of Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-His(5,Ser):
1.1.1.159; 1.1.1.178; 1.1.1.239; 1.1.1.35; 1.1.1.53; 1.1.1.62; 2.1.1.218; 2.1.1.221; 3.1.26.5;

The structure of Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-His(5,Ser) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-His(5,Ser) (pdb code 8cbk). 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 Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-His(5,Ser), PDB code: 8cbk:

Magnesium binding site 1 out of 1 in the Structure of Human Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-His(5,Ser)


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 Mitochondrial Rnase P in Complex with Mitochondrial Pre-Trna-His(5,Ser) within 5.0Å range: probe atom residue distance (Å) B Occ T:Mg201 b:174.6 occ:1.00 OP1 T:G1 1.9 183.3 1.0 OD2 E:ASP499 2.3 184.4 1.0 OE2 E:GLU477 3.0 213.4 1.0 P T:G1 3.1 189.3 1.0 O5' T:G1 3.3 183.0 1.0 CG E:ASP499 3.5 182.9 1.0 C5' T:G1 3.7 182.5 1.0 OD2 E:ASP503 3.7 177.4 1.0 OD1 E:ASP478 4.1 216.3 1.0 OP2 T:G1 4.1 184.3 1.0 CD E:GLU477 4.2 214.9 1.0 O3' T:U0 4.2 191.7 1.0 OD1 E:ASP499 4.3 184.5 1.0 OD2 E:ASP478 4.4 212.7 1.0 CB E:ASP499 4.4 178.8 1.0 CG E:ASP503 4.6 179.6 1.0 OE1 E:GLU477 4.7 214.7 1.0 CG E:ASP478 4.7 215.0 1.0 OD1 E:ASP503 4.7 181.5 1.0 CE E:MET501 4.7 183.1 1.0 C4' T:G1 4.9 181.5 1.0

V.Meynier, S.W.Hardwick, M.Catala, J.J.Roske, S.Oerum, D.Y.Chirgadze, P.Barraud, W.W.Yue, B.F.Luisi, C.Tisne. Structural Basis For Human Mitochondrial Trna Maturation. Nat Commun V. 15 4683 2024.
ISSN: ESSN 2041-1723
PubMed: 38824131
DOI: 10.1038/S41467-024-49132-0