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Manganese 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:

Magnesium (Mg) 1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total only one binding site of Manganese was determined in the Cryo-Em Structure of "Ct React" Conformation of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa, PDB code: 7zz1:

Manganese binding site 1 out of 1 in 7zz1

Go back to Manganese Binding Sites List in 7zz1
Manganese 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 Manganese with other atoms in the Mn 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:Mn1202

b:70.0
occ:1.00
OQ1 A:KCX703 2.2 58.5 1.0
O A:HOH1330 2.2 52.0 1.0
OQ2 A:KCX703 2.2 50.2 1.0
OD2 A:ASP534 2.2 55.8 1.0
NE2 A:HIS734 2.2 39.7 1.0
NE2 A:HIS732 2.2 37.7 1.0
CX A:KCX703 2.5 51.9 1.0
CG A:ASP534 3.0 40.4 1.0
CE1 A:HIS734 3.0 38.0 1.0
CE1 A:HIS732 3.2 43.0 1.0
CD2 A:HIS732 3.2 33.5 1.0
OD1 A:ASP534 3.2 47.7 1.0
CD2 A:HIS734 3.3 37.1 1.0
NE2 A:GLN768 3.7 47.7 1.0
NH2 A:ARG533 3.8 44.5 1.0
NZ A:KCX703 3.8 46.0 1.0
O A:HOH1304 4.0 60.1 1.0
ND1 A:HIS734 4.2 37.6 1.0
ND1 A:HIS732 4.3 41.0 1.0
CG A:HIS732 4.3 36.2 1.0
CB A:ASP534 4.4 31.9 1.0
CG A:HIS734 4.4 37.5 1.0
O A:HOH1332 4.4 48.0 1.0
O3 A:OAA1203 4.6 58.8 1.0
CD A:GLN768 4.7 43.1 1.0
CE A:KCX703 4.8 40.3 1.0
O1 A:OAA1203 4.8 66.3 1.0
OE1 A:GLN768 4.8 43.4 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: Sun Oct 6 11:15:02 2024

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