Magnesium in PDB 7zz0: Cryo-Em Structure of "Ct Empty" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa

Enzymatic activity of Cryo-Em Structure of "Ct Empty" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa

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

Other elements in 7zz0:

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

Manganese (Mn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of "Ct Empty" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa (pdb code 7zz0). 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 Cryo-Em Structure of "Ct Empty" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa, PDB code: 7zz0:

Magnesium binding site 1 out of 1 in 7zz0

Go back to Magnesium Binding Sites List in 7zz0
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of "Ct Empty" Conformation 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 Empty" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1201

b:54.1
occ:1.00
 O A:HOH1319 2.3 41.4 1.0
O A:THR522 2.4 50.0 1.0
O A:VAL519 2.7 52.0 1.0
OD2 A:ASP753 3.3 53.0 1.0
C A:THR522 3.5 48.4 1.0
C A:VAL519 3.9 42.6 1.0
O A:LYS520 4.0 58.4 1.0
NH2 A:ARG783 4.0 43.6 1.0
CG A:ASP753 4.1 52.8 1.0
O A:GLU524 4.1 56.1 1.0
CB A:ASP753 4.1 37.0 1.0
CA A:THR522 4.2 44.4 1.0
N A:THR522 4.2 45.8 1.0
CB A:THR522 4.2 45.2 1.0
C A:LYS520 4.3 46.2 1.0
CA A:ASP753 4.3 38.5 1.0
CA A:LYS520 4.4 36.4 1.0
N A:LYS520 4.6 37.7 1.0
N A:LYS523 4.6 56.1 1.0
CG1 A:VAL519 4.7 38.4 1.0
CA A:LYS523 4.8 55.3 1.0
CG2 A:THR522 4.8 49.2 1.0
C A:LYS523 4.9 55.0 1.0
O A:LYS523 4.9 60.5 1.0
O A:ASP753 4.9 45.4 1.0
CA A:VAL519 4.9 41.1 1.0

Reference:

J.P.Lopez-Alonso, M.Lazaro, D.Gil-Carton, P.H.Choi, 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
Page generated: Thu Oct 3 17:07:25 2024

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