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Magnesium in PDB 8c4o: Cdaa-Atp Complex

Enzymatic activity of Cdaa-Atp Complex

All present enzymatic activity of Cdaa-Atp Complex:
2.7.7.85;

Protein crystallography data

The structure of Cdaa-Atp Complex, PDB code: 8c4o was solved by P.Neumann, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.73 / 1.97
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.5, 64.65, 129.39, 90, 90, 90
R / Rfree (%) 23.5 / 25.4

Other elements in 8c4o:

The structure of Cdaa-Atp Complex also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Manganese (Mn) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cdaa-Atp Complex (pdb code 8c4o). 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 Cdaa-Atp Complex, PDB code: 8c4o:

Magnesium binding site 1 out of 1 in 8c4o

Go back to Magnesium Binding Sites List in 8c4o
Magnesium binding site 1 out of 1 in the Cdaa-Atp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cdaa-Atp Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg203

b:76.7
occ:1.00
OE2 B:GLU124 2.1 81.4 1.0
O1A B:ATP201 2.1 85.0 1.0
O2G B:ATP201 2.3 85.9 1.0
O2B B:ATP201 2.4 93.1 1.0
PA B:ATP201 3.1 92.5 1.0
CD B:GLU124 3.2 84.2 1.0
PB B:ATP201 3.3 92.0 1.0
HG3 B:GLU124 3.3 96.3 1.0
O3A B:ATP201 3.4 95.2 1.0
PG B:ATP201 3.4 77.0 1.0
O3B B:ATP201 3.4 83.5 1.0
CG B:GLU124 3.7 80.2 1.0
O2A B:ATP201 3.8 85.0 1.0
HG2 B:GLU124 4.0 96.3 1.0
O1G B:ATP201 4.1 76.2 1.0
OE1 B:GLU124 4.3 87.2 1.0
HA3 B:GLY101 4.5 100.9 1.0
O5' B:ATP201 4.5 83.0 1.0
O1B B:ATP201 4.7 79.6 1.0
H5'2 B:ATP201 4.7 99.2 1.0
O3G B:ATP201 4.7 73.1 1.0

Reference:

P.Neumann, P.Kloskowski, R.Ficner. Computer-Aided Design of A Cyclic Di-Amp Synthesizing Enzyme Cdaa Inhibitor. Microlife V. 4 AD021 2023.
ISSN: ISSN 2633-6693
PubMed: 37223749
DOI: 10.1093/FEMSML/UQAD021
Page generated: Thu Oct 3 20:07:13 2024

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