Magnesium in PDB 7zz1: Cryo-Em Structure of "Ct React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa

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

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

Other elements in 7zz1:

The structure of Cryo-Em Structure of "Ct React" 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 React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa (pdb code 7zz1). 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 React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa, PDB code: 7zz1:

Magnesium binding site 1 out of 1 in 7zz1

Go back to Magnesium Binding Sites List in 7zz1
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of "Ct React" 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 React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1201

b:47.1
occ:1.00
 O A:THR522 2.4 48.9 1.0
O A:HOH1313 2.5 43.4 1.0
O A:VAL519 2.6 50.0 1.0
OD2 A:ASP753 3.3 48.4 1.0
C A:THR522 3.5 44.5 1.0
C A:VAL519 3.8 38.6 1.0
CG A:ASP753 4.0 49.8 1.0
O A:LYS520 4.1 51.8 1.0
CB A:THR522 4.1 45.8 1.0
N A:THR522 4.1 43.1 1.0
NH2 A:ARG783 4.1 41.4 1.0
CA A:THR522 4.1 45.0 1.0
O A:GLU524 4.1 60.3 1.0
CB A:ASP753 4.2 38.9 1.0
C A:LYS520 4.2 44.3 1.0
CA A:LYS520 4.3 34.8 1.0
CA A:ASP753 4.3 32.6 1.0
N A:LYS520 4.5 31.6 1.0
CG1 A:VAL519 4.6 34.2 1.0
N A:LYS523 4.6 52.6 1.0
CA A:VAL519 4.8 32.5 1.0
O A:ASP753 4.9 39.6 1.0
CA A:LYS523 4.9 53.8 1.0
N A:ASN521 4.9 43.6 1.0
CG2 A:THR522 4.9 43.9 1.0
C A:LYS523 5.0 54.0 1.0
C A:ASN521 5.0 43.8 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 17:07:28 2024

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