Atomistry » Manganese » PDB 7z03-8awv » 7zz6
Atomistry »
  Manganese »
    PDB 7z03-8awv »
      7zz6 »

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

Enzymatic activity of 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;

Other elements in 7zz6:

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

Manganese Binding Sites:

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 7zz6

Go back to Manganese Binding Sites List in 7zz6
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 7zz6

Go back to Manganese Binding Sites List in 7zz6
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

Reference:

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
Page generated: Sun Oct 6 11:15:17 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy