Ytterbium in PDB 3b7t: [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate

All present enzymatic activity of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate:
3.3.2.6;

The structure of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate, PDB code: 3b7t was solved by F.Tholander, J.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)	30.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.490, 87.785, 99.916, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 27.3

The structure of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Ytterbium atom in the [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate (pdb code 3b7t). This binding sites where shown within 5.0 Angstroms radius around Ytterbium atom.
In total 2 binding sites of Ytterbium where determined in the [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate, PDB code: 3b7t:
Jump to Ytterbium binding site number: 1; 2;

Ytterbium binding site 1 out of 2 in the [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 1 of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Yb702 b:48.2 occ:1.00 OD2 A:ASP481 2.5 28.2 1.0 OD1 A:ASP481 2.5 33.2 1.0 O A:HOH709 2.8 43.4 1.0 CG A:ASP481 2.9 35.1 1.0 OD2 A:ASP482 4.2 45.8 1.0 OD1 A:ASP482 4.3 62.0 1.0 CB A:ASP481 4.4 32.0 1.0 CG A:ASP482 4.6 49.4 1.0 CB A:LYS479 4.7 43.2 1.0 CG A:LYS479 4.9 43.0 1.0

Ytterbium binding site 2 out of 2 in the [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 2 of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Yb703 b:0.8 occ:1.00 OD2 A:ASP175 2.7 81.3 1.0 CG A:ASP175 3.5 74.5 1.0 OD1 A:ASP175 3.7 70.0 1.0 O A:ASP175 4.5 55.8 1.0 CB A:ASP175 4.7 63.7 1.0 CA A:ASP175 4.8 57.4 1.0 C A:ASP175 4.9 59.8 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