Lutetium in PDB 2pes: Urate Oxidase in Complex with Tris-Dipicolinate Lutetium

All present enzymatic activity of Urate Oxidase in Complex with Tris-Dipicolinate Lutetium:
1.7.3.3;

The structure of Urate Oxidase in Complex with Tris-Dipicolinate Lutetium, PDB code: 2pes was solved by G.Pompidor, J.Vicat, R.Kahn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.60
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	79.550, 95.320, 104.330, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 19.5

The binding sites of Lutetium atom in the Urate Oxidase in Complex with Tris-Dipicolinate Lutetium (pdb code 2pes). This binding sites where shown within 5.0 Angstroms radius around Lutetium atom.
In total 3 binding sites of Lutetium where determined in the Urate Oxidase in Complex with Tris-Dipicolinate Lutetium, PDB code: 2pes:
Jump to Lutetium binding site number: 1; 2; 3;

Lutetium binding site 1 out of 3 in the Urate Oxidase in Complex with Tris-Dipicolinate Lutetium


Mono view


Stereo pair view

A full contact list of Lutetium with other atoms in the Lu binding site number 1 of Urate Oxidase in Complex with Tris-Dipicolinate Lutetium within 5.0Å range: probe atom residue distance (Å) B Occ A:Lu296 b:26.4 occ:0.46 O3 A:PDC304 2.3 33.0 0.5 N1 A:PDC304 2.3 32.1 0.5 O1 A:PDC303 2.3 22.4 0.5 N1 A:PDC303 2.4 26.3 0.5 N1 A:PDC302 2.4 25.5 0.5 O1 A:PDC302 2.5 27.3 0.5 O3 A:PDC303 2.5 25.9 0.5 O3 A:PDC302 2.6 28.8 0.5 O1 A:PDC304 2.6 33.0 0.5 C8 A:PDC304 3.1 33.3 0.5 C6 A:PDC304 3.1 32.7 0.5 C7 A:PDC303 3.2 25.5 0.5 C2 A:PDC303 3.2 26.4 0.5 C2 A:PDC304 3.3 32.5 0.5 C2 A:PDC302 3.3 25.9 0.5 C6 A:PDC302 3.3 27.1 0.5 C6 A:PDC303 3.3 26.9 0.5 C7 A:PDC302 3.3 26.0 0.5 C8 A:PDC302 3.3 27.5 0.5 C8 A:PDC303 3.3 26.9 0.5 C7 A:PDC304 3.4 32.5 0.5 O4 A:PDC304 4.3 33.1 0.5 O2 A:PDC303 4.4 25.9 0.5 C5 A:PDC304 4.5 32.6 0.5 O2 A:PDC302 4.5 24.2 0.5 O4 A:PDC302 4.5 28.1 0.5 NZ A:LYS203 4.5 29.0 1.0 C3 A:PDC303 4.5 26.8 0.5 O4 A:PDC303 4.5 28.3 0.5 C3 A:PDC304 4.6 32.0 0.5 O2 A:PDC304 4.6 32.5 0.5 C5 A:PDC303 4.6 26.2 0.5 C3 A:PDC302 4.6 25.8 0.5 C5 A:PDC302 4.6 25.1 0.5 CE A:LYS203 5.0 28.7 1.0

Lutetium binding site 2 out of 3 in the Urate Oxidase in Complex with Tris-Dipicolinate Lutetium


Mono view


Stereo pair view

A full contact list of Lutetium with other atoms in the Lu binding site number 2 of Urate Oxidase in Complex with Tris-Dipicolinate Lutetium within 5.0Å range: probe atom residue distance (Å) B Occ A:Lu297 b:26.0 occ:0.36 O1 A:PDC305 2.2 27.2 0.4 N1 A:PDC307 2.3 30.5 0.4 N1 A:PDC305 2.3 26.4 0.4 N1 A:PDC306 2.4 26.0 0.4 O1 A:PDC306 2.5 26.0 0.4 O1 A:PDC307 2.5 32.2 0.4 O3 A:PDC307 2.6 29.9 0.4 O3 A:PDC305 2.6 26.9 0.4 O3 A:PDC306 2.7 25.0 0.4 C7 A:PDC305 3.1 27.5 0.4 C2 A:PDC305 3.1 26.7 0.4 C2 A:PDC307 3.2 31.4 0.4 C7 A:PDC307 3.2 32.2 0.4 C6 A:PDC307 3.2 30.4 0.4 C2 A:PDC306 3.2 25.4 0.4 C7 A:PDC306 3.2 26.1 0.4 C6 A:PDC306 3.3 24.9 0.4 C8 A:PDC307 3.3 30.4 0.4 C6 A:PDC305 3.3 26.6 0.4 C8 A:PDC306 3.3 25.1 0.4 C8 A:PDC305 3.4 26.5 0.4 O2 A:PDC305 4.3 29.2 0.4 O2 A:PDC307 4.4 32.6 0.4 O4 A:PDC306 4.4 24.6 0.4 O2 A:PDC306 4.5 25.8 0.4 C3 A:PDC305 4.5 26.3 0.4 C3 A:PDC307 4.5 31.1 0.4 O4 A:PDC307 4.5 30.3 0.4 C5 A:PDC307 4.5 30.7 0.4 C3 A:PDC306 4.6 24.9 0.4 C5 A:PDC305 4.6 26.6 0.4 O4 A:PDC305 4.6 27.0 0.4 C5 A:PDC306 4.6 24.9 0.4

Lutetium binding site 3 out of 3 in the Urate Oxidase in Complex with Tris-Dipicolinate Lutetium


Mono view


Stereo pair view

A full contact list of Lutetium with other atoms in the Lu binding site number 3 of Urate Oxidase in Complex with Tris-Dipicolinate Lutetium within 5.0Å range:

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