Praseodymium in PDB 2wvi: Crystal Structure of the N-Terminal Domain of BUBR1

All present enzymatic activity of Crystal Structure of the N-Terminal Domain of BUBR1:
2.7.11.1;

The structure of Crystal Structure of the N-Terminal Domain of BUBR1, PDB code: 2wvi was solved by S.D'arcy, O.R.Davies, T.L.Blundell, V.M.Bolanos-Garcia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.39 / 1.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	62.796, 62.796, 90.450, 90.00, 90.00, 120.00
R / Rfree (%)	22.188 / 25.986

The binding sites of Praseodymium atom in the Crystal Structure of the N-Terminal Domain of BUBR1 (pdb code 2wvi). This binding sites where shown within 5.0 Angstroms radius around Praseodymium atom.
In total 2 binding sites of Praseodymium where determined in the Crystal Structure of the N-Terminal Domain of BUBR1, PDB code: 2wvi:
Jump to Praseodymium binding site number: 1; 2;

Praseodymium binding site 1 out of 2 in the Crystal Structure of the N-Terminal Domain of BUBR1


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 1 of Crystal Structure of the N-Terminal Domain of BUBR1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Pr1221 b:23.4 occ:1.00 OE1 A:GLU218 1.5 13.9 1.0 CD A:GLU218 2.4 26.7 1.0 O A:ACT1223 2.5 20.9 1.0 OXT A:ACT1223 2.6 24.0 1.0 OE2 A:GLU218 2.6 18.4 1.0 OE2 A:GLU215 2.6 22.4 1.0 OE2 A:GLU214 2.6 20.1 1.0 OE1 A:GLU214 2.6 29.4 1.0 C A:ACT1223 2.8 20.4 1.0 CD A:GLU214 3.0 27.2 1.0 CD A:GLU215 3.8 25.0 1.0 CG A:GLU218 4.0 28.2 1.0 O A:HOH2114 4.0 22.0 1.0 PR A:PR1222 4.1 20.6 1.0 CH3 A:ACT1223 4.3 15.6 1.0 CG A:GLU215 4.5 22.9 1.0 CG A:GLU214 4.5 27.9 1.0 OE1 A:GLU215 4.7 17.9 1.0 O A:HOH2117 4.8 29.6 1.0 CA A:GLU215 4.9 27.5 1.0 O A:HOH2113 4.9 31.9 1.0

Praseodymium binding site 2 out of 2 in the Crystal Structure of the N-Terminal Domain of BUBR1


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 2 of Crystal Structure of the N-Terminal Domain of BUBR1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Pr1222 b:20.6 occ:1.00 O A:HOH2114 2.3 22.0 1.0 O A:ACT1223 2.5 20.9 1.0 OE2 A:GLU215 2.5 22.4 1.0 OE1 A:GLU215 2.6 17.9 1.0 CD A:GLU215 3.0 25.0 1.0 C A:ACT1223 3.5 20.4 1.0 CH3 A:ACT1223 3.8 15.6 1.0 PR A:PR1221 4.1 23.4 1.0 OE1 A:GLU218 4.2 13.9 1.0 CG A:GLU215 4.5 22.9 1.0 OXT A:ACT1223 4.6 24.0 1.0 C2 A:EDO1225 4.9 48.0 1.0

S.D'arcy, O.R.Davies, T.L.Blundell, V.M.Bolanos-Garcia. Defining the Molecular Basis of BUBR1 Kinetochore Interactions and Anaphase-Promoting Complex/Cyclosome (Apc/C)-CDC20 Inhibition J.Biol.Chem. V. 285 14764 2010.
ISSN: ISSN 0021-9258
PubMed: 20220147
DOI: 10.1074/JBC.M109.082016