Zinc 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:

Ytterbium

(Yb)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate, PDB code: 3b7t:

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn 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:Zn701 b:41.0 occ:1.00 NE2 A:HIS295 2.1 34.4 1.0 OE1 A:GLU318 2.1 40.7 1.0 NE2 A:HIS299 2.2 39.5 1.0 N B:ARG702 2.3 58.8 1.0 O B:ARG702 2.5 42.8 1.0 OE2 A:GLU318 2.6 49.8 1.0 CD A:GLU318 2.7 44.0 1.0 C B:ARG702 2.9 44.1 1.0 CA B:ARG702 3.0 47.5 1.0 CE1 A:HIS295 3.0 42.6 1.0 CE1 A:HIS299 3.1 35.3 1.0 CD2 A:HIS295 3.1 34.6 1.0 CD2 A:HIS299 3.2 34.3 1.0 N B:ALA703 4.0 44.5 1.0 OE2 A:GLU271 4.1 80.6 1.0 ND1 A:HIS295 4.2 35.8 1.0 CG A:GLU318 4.2 45.8 1.0 CE2 A:TYR383 4.2 39.7 1.0 CG A:HIS295 4.2 44.8 1.0 ND1 A:HIS299 4.2 46.8 1.0 CG A:HIS299 4.3 33.6 1.0 CB B:ARG702 4.4 58.6 1.0 OH A:TYR383 4.5 46.1 1.0 CG2 A:THR321 4.5 39.0 1.0 CD A:GLU271 4.7 66.7 1.0 CA B:ALA703 4.7 50.2 1.0 OE1 A:GLU271 4.7 60.0 1.0 CZ A:TYR383 4.9 44.5 1.0 CB A:GLU318 4.9 42.0 1.0 CG B:ARG702 4.9 51.8 1.0 CA A:GLU318 5.0 40.4 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