Manganese 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:

Magnesium

(Mg)

2 atoms

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa, PDB code: 7zz6:
Jump to Manganese binding site number: 1; 2;

Manganese 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 Manganese with other atoms in the Mn 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:Mn1202 b:29.6 occ:1.00 NE2 D:HIS732 1.8 22.6 1.0 O D:HOH1335 2.2 25.1 1.0 NE2 D:HIS734 2.2 24.0 1.0 OD2 D:ASP534 2.2 23.4 1.0 OQ2 D:KCX703 2.4 25.2 1.0 OQ1 D:KCX703 2.4 25.2 1.0 CE1 D:HIS732 2.6 22.6 1.0 CX D:KCX703 2.7 25.2 1.0 CD2 D:HIS732 3.0 22.6 1.0 CD2 D:HIS734 3.1 24.0 1.0 CE1 D:HIS734 3.3 24.0 1.0 CG D:ASP534 3.3 23.4 1.0 NE2 D:GLN768 3.5 22.5 1.0 OD1 D:ASP534 3.7 23.4 1.0 ND1 D:HIS732 3.8 22.6 1.0 O D:HOH1360 3.9 31.9 1.0 CG D:HIS732 4.0 22.6 1.0 NZ D:KCX703 4.0 25.2 1.0 NH2 D:ARG533 4.2 23.7 1.0 O D:HOH1332 4.3 25.7 1.0 CG D:HIS734 4.3 24.0 1.0 ND1 D:HIS734 4.3 24.0 1.0 CB D:ASP534 4.6 23.4 1.0 CD D:GLN768 4.6 22.5 1.0 O3 D:PYR1203 4.7 31.0 1.0 CA D:MET705 4.8 29.2 1.0 CE D:KCX703 4.9 25.2 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn1202 b:32.7 occ:1.00 NE2 A:HIS732 1.8 25.7 1.0 O A:HOH1333 2.2 27.9 1.0 NE2 A:HIS734 2.2 26.3 1.0 OD2 A:ASP534 2.2 25.1 1.0 OQ1 A:KCX703 2.4 29.2 1.0 OQ2 A:KCX703 2.4 29.2 1.0 CE1 A:HIS732 2.6 25.7 1.0 CX A:KCX703 2.7 29.2 1.0 CD2 A:HIS732 3.0 25.7 1.0 CD2 A:HIS734 3.1 26.3 1.0 CE1 A:HIS734 3.2 26.3 1.0 CG A:ASP534 3.3 25.1 1.0 NE2 A:GLN768 3.6 24.3 1.0 OD1 A:ASP534 3.7 25.1 1.0 ND1 A:HIS732 3.8 25.7 1.0 O A:HOH1347 3.9 34.2 1.0 CG A:HIS732 4.0 25.7 1.0 NZ A:KCX703 4.0 29.2 1.0 NH2 A:ARG533 4.2 25.6 1.0 CG A:HIS734 4.3 26.3 1.0 ND1 A:HIS734 4.3 26.3 1.0 O A:HOH1313 4.4 29.4 1.0 CB A:ASP534 4.6 25.1 1.0 CD A:GLN768 4.6 24.3 1.0 CA A:MET705 4.8 33.1 1.0 O3 A:PYR1203 4.8 34.4 1.0 CE A:KCX703 4.9 29.2 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