Magnesium in PDB 7zz6: Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa

All present enzymatic activity of Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa:
6.4.1.1;

The structure of Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Magnesium atom in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa (pdb code 7zz6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa, PDB code: 7zz6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1201 b:29.6 occ:1.00 O D:VAL519 2.5 28.6 1.0 O D:HOH1346 2.6 26.8 1.0 OD1 D:ASP753 2.6 25.7 1.0 O D:THR522 2.6 28.8 1.0 CG D:ASP753 3.6 25.7 1.0 C D:VAL519 3.7 28.6 1.0 C D:THR522 3.7 28.8 1.0 O D:LYS520 3.8 29.4 1.0 CB D:ASP753 4.1 25.7 1.0 C D:LYS520 4.1 29.4 1.0 N D:THR522 4.1 28.8 1.0 CA D:LYS520 4.2 29.4 1.0 CA D:ASP753 4.3 25.7 1.0 CA D:THR522 4.3 28.8 1.0 CB D:THR522 4.3 28.8 1.0 N D:LYS520 4.4 29.4 1.0 O D:GLU524 4.4 28.8 1.0 NH2 D:ARG783 4.5 25.6 1.0 CG1 D:VAL519 4.6 28.6 1.0 OD2 D:ASP753 4.6 25.7 1.0 CA D:VAL519 4.8 28.6 1.0 N D:ASN521 4.8 29.6 1.0 N D:LYS523 4.9 29.4 1.0 O D:ASP753 5.0 25.7 1.0

Magnesium binding site 2 out of 2 in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1201 b:33.6 occ:1.00 OD2 A:ASP753 1.4 30.7 1.0 CG A:ASP753 2.4 30.7 1.0 O A:VAL519 2.6 32.8 1.0 O A:HOH1301 2.7 30.3 1.0 O A:THR522 2.7 33.0 1.0 OD1 A:ASP753 2.8 30.7 1.0 CB A:ASP753 3.7 30.7 1.0 O A:LYS520 3.7 34.4 1.0 C A:VAL519 3.7 32.8 1.0 C A:THR522 3.9 33.0 1.0 C A:LYS520 4.0 34.4 1.0 CA A:LYS520 4.1 34.4 1.0 CA A:ASP753 4.3 30.7 1.0 N A:THR522 4.3 33.0 1.0 N A:LYS520 4.4 34.4 1.0 CA A:THR522 4.5 33.0 1.0 CB A:THR522 4.6 33.0 1.0 NH2 A:ARG783 4.6 28.7 1.0 O A:GLU524 4.6 32.1 1.0 CG1 A:VAL519 4.7 32.8 1.0 N A:ASN521 4.9 34.4 1.0 CA A:VAL519 4.9 32.8 1.0 N A:LYS523 5.0 33.5 1.0

J.P.Lopez-Alonso, M.Lazaro, D.Gil-Carton, P.H.Choi, A.Dodu, L.Tong, M.Valle. Cryoem Structural Exploration of Catalytically Active Enzyme Pyruvate Carboxylase. Nat Commun V. 13 6185 2022.
ISSN: ESSN 2041-1723
PubMed: 36261450
DOI: 10.1038/S41467-022-33987-2