Ytterbium in PDB 2r59: Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041

All present enzymatic activity of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041:
3.3.2.6;

The structure of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041, PDB code: 2r59 was solved by F.Tholander, J.Z.Haeggstrom, M.Thunnissen, A.Muroya, B.P.Roques, M.C.Fournie-Zaluski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.85 / 1.89
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.210, 87.230, 99.230, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 22.7

The structure of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Ytterbium atom in the Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041 (pdb code 2r59). This binding sites where shown within 5.0 Angstroms radius around Ytterbium atom.
In total only one binding site of Ytterbium was determined in the Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041, PDB code: 2r59:

Ytterbium binding site 1 out of 1 in the Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 1 of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041 within 5.0Å range: probe atom residue distance (Å) B Occ A:Yb705 b:23.7 occ:1.00 O A:HOH1034 2.0 17.5 1.0 OD1 A:ASP481 2.3 19.5 1.0 OD2 A:ASP481 2.3 22.7 1.0 O A:HOH770 2.4 19.2 1.0 CG A:ASP481 2.6 21.0 1.0 CB A:ASP481 4.2 19.8 1.0 OD2 A:ASP482 4.4 22.6 1.0 OD1 A:ASP482 4.5 24.5 1.0 CG A:ASP482 4.8 25.8 1.0 CB A:LYS479 4.8 19.6 1.0 CG A:LYS479 4.9 20.8 1.0

F.Tholander, A.Muroya, B.P.Roques, M.C.Fournie-Zaluski, M.M.Thunnissen, J.Z.Haeggstrom. Structure-Based Dissection of the Active Site Chemistry of Leukotriene A4 Hydrolase: Implications For M1 Aminopeptidases and Inhibitor Design. Chem.Biol. V. 15 920 2008.
ISSN: ISSN 1074-5521
PubMed: 18804029
DOI: 10.1016/J.CHEMBIOL.2008.07.018