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Europium in PDB 3ojo: Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus

Protein crystallography data

The structure of Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus, PDB code: 3ojo was solved by S.Nessler, J.Gruszczyk, V.Olivares-Illana, P.Meyer, S.Morera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.63 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.220, 131.497, 158.820, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 24.6

Europium Binding Sites:

The binding sites of Europium atom in the Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus (pdb code 3ojo). This binding sites where shown within 5.0 Angstroms radius around Europium atom.
In total 2 binding sites of Europium where determined in the Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus, PDB code: 3ojo:
Jump to Europium binding site number: 1; 2;

Europium binding site 1 out of 2 in 3ojo

Go back to Europium Binding Sites List in 3ojo
Europium binding site 1 out of 2 in the Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 1 of Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Eu501

b:33.2
occ:0.53
O2 B:PDC504 1.5 79.1 1.0
O1 B:PDC502 1.7 46.0 1.0
N1 B:PDC504 2.0 75.6 1.0
N1 B:PDC502 2.3 47.0 0.8
O2 B:PDC503 2.3 54.7 1.0
C7 B:PDC504 2.3 75.5 1.0
O4 B:PDC503 2.5 51.2 1.0
C2 B:PDC504 2.5 74.5 1.0
C7 B:PDC502 2.6 46.5 0.9
C2 B:PDC502 2.9 45.8 0.7
N1 B:PDC503 2.9 51.4 1.0
C6 B:PDC504 3.1 75.8 1.0
O4 B:PDC502 3.3 49.4 1.0
C7 B:PDC503 3.4 51.2 1.0
C6 B:PDC502 3.4 47.4 1.0
O4 B:PDC504 3.4 76.5 1.0
C8 B:PDC503 3.5 52.4 1.0
O1 B:PDC504 3.5 75.4 1.0
C2 B:PDC503 3.6 50.2 1.0
C6 B:PDC503 3.7 51.5 1.0
C8 B:PDC504 3.7 76.7 1.0
C8 B:PDC502 3.8 48.9 0.4
C3 B:PDC504 3.9 72.5 1.0
O2 B:PDC502 4.0 50.1 1.0
C3 B:PDC502 4.3 43.8 1.0
C5 B:PDC504 4.3 73.5 1.0
O1 B:PDC503 4.5 50.9 1.0
O3 B:PDC503 4.6 54.9 1.0
C4 B:PDC504 4.6 72.6 1.0
C5 B:PDC502 4.7 45.0 0.9
CE1 A:HIS242 4.7 42.1 1.0
NH2 A:ARG244 4.7 67.3 1.0
O3 B:PDC504 4.9 78.8 1.0
C3 B:PDC503 5.0 48.2 1.0

Europium binding site 2 out of 2 in 3ojo

Go back to Europium Binding Sites List in 3ojo
Europium binding site 2 out of 2 in the Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 2 of Derivative Structure of the Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O From S. Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Eu501

b:22.0
occ:0.44
O1 A:PDC503 1.4 38.7 0.8
O4 A:PDC502 1.8 52.3 1.0
O4 A:PDC504 2.0 39.1 1.0
N1 A:PDC503 2.3 39.5 0.6
N1 A:PDC502 2.4 51.7 0.8
C7 A:PDC503 2.4 39.1 1.0
C2 A:PDC503 2.7 38.4 1.0
N1 A:PDC504 2.8 39.4 0.9
C8 A:PDC502 2.9 52.3 1.0
O1 A:PDC502 2.9 52.2 1.0
C6 A:PDC502 3.1 51.8 1.0
O1 A:PDC504 3.1 39.5 1.0
C8 A:PDC504 3.1 40.0 0.8
C2 A:PDC502 3.4 50.6 1.0
C6 A:PDC504 3.5 39.5 1.0
C6 A:PDC503 3.5 39.7 1.0
O4 A:PDC503 3.6 42.2 1.0
C7 A:PDC502 3.6 52.1 1.0
O2 A:PDC503 3.7 42.7 0.8
C2 A:PDC504 3.8 38.3 1.0
C7 A:PDC504 3.9 39.5 1.0
O3 A:PDC502 4.1 53.5 1.0
C8 A:PDC503 4.1 40.7 1.0
C3 A:PDC503 4.2 36.4 0.8
O3 A:PDC504 4.2 41.7 0.9
C5 A:PDC502 4.5 49.6 0.6
O A:HOH427 4.5 37.5 1.0
NH1 B:ARG244 4.5 70.9 1.0
C3 A:PDC502 4.7 48.6 0.9
C5 A:PDC503 4.7 37.4 1.0
CE1 B:HIS242 4.8 39.5 1.0
C5 A:PDC504 4.9 37.2 0.4
O2 A:PDC502 4.9 55.7 1.0
NH2 A:ARG211 5.0 61.3 1.0
C4 A:PDC503 5.0 36.4 0.9

Reference:

J.Gruszczyk, A.Fleurie, V.Olivares-Illana, E.Bechet, I.Zanella-Cleon, S.Morera, P.Meyer, G.Pompidor, R.Kahn, C.Grangeasse, S.Nessler. Structure Analysis of the Staphylococcus Aureus Udp-N-Acetyl-Mannosamine Dehydrogenase CAP5O Involved in Capsular Polysaccharide Biosynthesis. J.Biol.Chem. V. 286 17112 2011.
ISSN: ISSN 0021-9258
PubMed: 21454499
DOI: 10.1074/JBC.M110.216002
Page generated: Wed Jul 31 10:40:52 2024

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