Zinc in PDB 2xq0: Structure of Yeast LTA4 Hydrolase in Complex with Bestatin

All present enzymatic activity of Structure of Yeast LTA4 Hydrolase in Complex with Bestatin:
3.3.2.6;

The structure of Structure of Yeast LTA4 Hydrolase in Complex with Bestatin, PDB code: 2xq0 was solved by C.Helgstrand, M.Hasan, H.Usyal, J.Z.Haeggstrom, M.M.G.M.Thunnissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.66 / 1.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.641, 99.874, 112.651, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 24.8

The structure of Structure of Yeast LTA4 Hydrolase in Complex with Bestatin also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Zinc atom in the Structure of Yeast LTA4 Hydrolase in Complex with Bestatin (pdb code 2xq0). 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 Structure of Yeast LTA4 Hydrolase in Complex with Bestatin, PDB code: 2xq0:

Zinc binding site 1 out of 1 in the Structure of Yeast LTA4 Hydrolase in Complex with Bestatin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Yeast LTA4 Hydrolase in Complex with Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1672 b:30.6 occ:1.00 NE2 A:HIS344 2.0 19.1 1.0 NE2 A:HIS340 2.2 21.8 1.0 OE1 A:GLU363 2.2 31.9 1.0 O2 A:BES901 2.4 32.4 1.0 O3 A:BES901 2.4 38.3 1.0 OE2 A:GLU363 2.7 45.9 1.0 CD A:GLU363 2.8 36.3 1.0 CE1 A:HIS344 3.0 17.8 1.0 C3 A:BES901 3.0 47.6 1.0 CD2 A:HIS340 3.0 26.6 1.0 CD2 A:HIS344 3.0 22.0 1.0 C2 A:BES901 3.1 44.9 1.0 CE1 A:HIS340 3.3 25.9 1.0 C1 A:BES901 3.8 45.9 1.0 CE2 A:TYR429 4.1 25.9 1.0 ND1 A:HIS344 4.1 18.5 1.0 CG A:HIS344 4.2 16.8 1.0 CG A:HIS340 4.2 27.8 1.0 N1 A:BES901 4.3 55.0 1.0 OE1 A:GLU316 4.3 27.9 1.0 ND1 A:HIS340 4.3 25.1 1.0 CG2 A:THR366 4.3 14.1 1.0 CG A:GLU363 4.3 27.8 1.0 OH A:TYR429 4.5 33.5 1.0 N2 A:BES901 4.5 46.8 1.0 CD A:GLU316 4.7 26.4 1.0 CB A:THR366 4.7 16.4 1.0 OE2 A:GLU316 4.8 32.3 1.0 CZ A:TYR429 4.8 32.5 1.0 O A:HOH2222 4.8 34.5 1.0 C16 A:BES901 4.9 59.0 1.0 OE2 A:GLU341 4.9 57.0 1.0 OG1 A:THR366 5.0 21.9 1.0 C6 A:BES901 5.0 46.7 1.0

C.Helgstrand, M.Hasan, H.Usyal, J.Z.Haeggstrom, M.M.G.M.Thunnissen. A Leukotriene A(4) Hydrolase-Related Aminopeptidase From Yeast Undergoes Induced Fit Upon Inhibitor Binding. J.Mol.Biol. V. 406 120 2011.
ISSN: ISSN 0022-2836
PubMed: 21146536
DOI: 10.1016/J.JMB.2010.11.059