Europium in PDB 3lgr: Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium

All present enzymatic activity of Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium:
3.2.1.8;

The structure of Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium, PDB code: 3lgr was solved by G.Pompidor, R.Kahn, O.Maury, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.51 / 1.64
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	110.890, 38.370, 47.590, 90.00, 99.83, 90.00
R / Rfree (%)	13.8 / 16.8

The binding sites of Europium atom in the Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium (pdb code 3lgr). This binding sites where shown within 5.0 Angstroms radius around Europium atom.
In total 3 binding sites of Europium where determined in the Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium, PDB code: 3lgr:
Jump to Europium binding site number: 1; 2; 3;

Europium binding site 1 out of 3 in the Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 1 of Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu201 b:11.6 occ:0.50 O1 A:PDC303 2.3 6.5 0.5 O4 A:PDC302 2.3 6.7 0.5 O1 A:PDC302 2.4 9.7 0.5 O1 A:PDC304 2.4 8.3 0.5 O4 A:PDC304 2.5 8.7 0.5 O4 A:PDC303 2.5 10.9 0.5 N1 A:PDC303 2.6 11.1 0.5 N1 A:PDC302 2.6 10.0 0.5 N1 A:PDC304 2.7 7.8 0.5 C7 A:PDC303 3.3 8.6 0.5 C8 A:PDC302 3.3 8.4 0.5 C7 A:PDC302 3.4 9.6 0.5 C7 A:PDC304 3.4 7.5 0.5 C8 A:PDC303 3.4 11.8 0.5 C8 A:PDC304 3.4 7.2 0.5 C2 A:PDC303 3.5 6.3 0.5 C6 A:PDC302 3.5 5.9 0.5 C6 A:PDC304 3.5 5.0 0.5 C2 A:PDC304 3.5 5.0 0.5 C6 A:PDC303 3.5 10.3 0.5 C2 A:PDC302 3.5 8.6 0.5 O A:HOH351 4.5 7.0 1.0 O2 A:PDC303 4.5 9.4 0.5 O3 A:PDC302 4.5 9.4 0.5 O A:HOH383 4.5 10.1 1.0 O2 A:PDC302 4.5 8.8 0.5 O2 A:PDC304 4.6 7.6 0.5 O3 A:PDC303 4.6 12.6 0.5 O3 A:PDC304 4.6 7.7 0.5 C5 A:PDC302 4.8 7.1 0.5 C3 A:PDC303 4.8 7.7 0.5 C3 A:PDC304 4.9 6.8 0.5 C5 A:PDC304 4.9 6.4 0.5 C5 A:PDC303 4.9 11.2 0.5 C3 A:PDC302 4.9 9.8 0.5

Europium binding site 2 out of 3 in the Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 2 of Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu202 b:13.9 occ:0.10 O A:HOH311 4.3 32.4 1.0 O A:HOH227 4.5 19.4 1.0

Europium binding site 3 out of 3 in the Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 3 of Xylanase II From Trichoderma Reesei Cocrystallized with Tris- Dipicolinate Europium within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu203 b:15.6 occ:0.10 O A:HOH331 2.5 35.2 1.0 O A:HOH544 2.6 23.2 1.0 O A:HOH374 3.8 39.9 1.0 O A:HOH273 3.9 24.9 1.0 O A:HOH536 4.0 26.5 1.0 O A:HOH390 4.3 15.2 1.0 NE1 A:TRP18 4.7 18.7 1.0 CB A:PRO126 4.9 9.2 1.0 O A:HOH346 4.9 42.8 1.0

G.Pompidor, O.Maury, J.Vicat, R.Kahn. A Dipicolinate Lanthanide Complex For Solving Protein Structures Using Anomalous Diffraction. Acta Crystallogr.,Sect.D V. 66 762 2010.
ISSN: ISSN 0907-4449
PubMed: 20606256
DOI: 10.1107/S0907444910010954