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Manganese in PDB 8po5: Lactobacillus Plantarum Lpdd

Protein crystallography data

The structure of Lactobacillus Plantarum Lpdd, PDB code: 8po5 was solved by D.Gahloth, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.03 / 2.10
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.5, 92.98, 126.82, 90, 90, 90
R / Rfree (%) 19.5 / 25.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Lactobacillus Plantarum Lpdd (pdb code 8po5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Lactobacillus Plantarum Lpdd, PDB code: 8po5:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 8po5

Go back to Manganese Binding Sites List in 8po5
Manganese binding site 1 out of 2 in the Lactobacillus Plantarum Lpdd


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Lactobacillus Plantarum Lpdd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:38.9
occ:1.00
OD2 A:ASP63 2.0 36.3 1.0
ND1 A:HIS61 2.1 61.0 1.0
NE2 A:HIS35 2.3 34.5 1.0
O A:HOH351 2.6 45.6 1.0
CE1 A:HIS61 2.9 53.9 1.0
CG A:ASP63 3.0 37.4 1.0
CG A:HIS61 3.1 52.4 1.0
O A:HOH357 3.1 38.6 1.0
CE1 A:HIS35 3.1 39.9 1.0
CD2 A:HIS35 3.3 32.0 1.0
OD1 A:ASP63 3.3 32.0 1.0
CB A:HIS61 3.5 44.9 1.0
NE2 A:HIS61 4.1 46.0 1.0
CD2 A:HIS61 4.2 43.8 1.0
CA A:HIS61 4.2 52.2 1.0
ND1 A:HIS35 4.3 38.2 1.0
CB A:ASP63 4.3 26.5 1.0
CG A:HIS35 4.4 34.0 1.0
CA A:GLY37 4.4 29.3 1.0
N A:LYS62 4.5 50.4 1.0
N A:ASP63 4.6 38.6 1.0
O A:ILE88 4.6 38.4 1.0
C A:HIS61 4.8 46.8 1.0
CA A:GLY87 4.9 35.8 1.0

Manganese binding site 2 out of 2 in 8po5

Go back to Manganese Binding Sites List in 8po5
Manganese binding site 2 out of 2 in the Lactobacillus Plantarum Lpdd


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Lactobacillus Plantarum Lpdd within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn201

b:33.9
occ:1.00
OD2 B:ASP63 2.0 37.0 1.0
ND1 B:HIS61 2.0 37.9 1.0
NE2 B:HIS35 2.1 30.4 1.0
O B:HOH362 2.7 44.6 1.0
CE1 B:HIS61 2.9 38.3 1.0
CG B:ASP63 3.0 34.7 1.0
CE1 B:HIS35 3.1 32.7 1.0
CG B:HIS61 3.1 34.0 1.0
CD2 B:HIS35 3.1 30.7 1.0
O B:HOH365 3.2 38.0 1.0
OD1 B:ASP63 3.3 33.0 1.0
CB B:HIS61 3.6 33.1 1.0
NE2 B:HIS61 4.0 35.9 1.0
CD2 B:HIS61 4.2 35.7 1.0
ND1 B:HIS35 4.2 33.4 1.0
CG B:HIS35 4.3 30.0 1.0
CA B:HIS61 4.3 38.5 1.0
CB B:ASP63 4.3 27.4 1.0
CA B:GLY37 4.5 29.7 1.0
N B:LYS62 4.5 44.9 1.0
O B:ILE88 4.6 34.9 1.0
N B:ASP63 4.7 33.9 1.0
C B:HIS61 4.9 43.8 1.0
CA B:GLY87 5.0 26.9 1.0
N B:ILE88 5.0 33.6 1.0

Reference:

D.Gahloth, D.Leys. Gallate Decarboxylase Subunit D, Lpdd To Be Published.
Page generated: Sun Oct 6 13:31:49 2024

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