Zinc in PDB 2xpz: Structure of Native Yeast LTA4 Hydrolase

All present enzymatic activity of Structure of Native Yeast LTA4 Hydrolase:
3.3.2.6;

The structure of Structure of Native Yeast LTA4 Hydrolase, PDB code: 2xpz 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)	14.98 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.833, 98.096, 99.197, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 26.9

The binding sites of Zinc atom in the Structure of Native Yeast LTA4 Hydrolase (pdb code 2xpz). 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 Native Yeast LTA4 Hydrolase, PDB code: 2xpz:

Zinc binding site 1 out of 1 in the Structure of Native Yeast LTA4 Hydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Native Yeast LTA4 Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1673 b:32.0 occ:1.00 OE2 A:GLU363 2.1 52.2 1.0 NE2 A:HIS340 2.1 32.7 1.0 NE2 A:HIS344 2.3 21.4 1.0 OE1 A:GLU363 2.7 56.8 1.0 CD A:GLU363 2.8 50.6 1.0 CD2 A:HIS340 3.0 23.9 1.0 CD2 A:HIS344 3.1 20.3 1.0 O A:HOH2286 3.1 45.6 1.0 CE1 A:HIS340 3.2 31.8 1.0 CE1 A:HIS344 3.4 21.3 1.0 O A:HOH2164 4.0 46.4 1.0 CE2 A:TYR429 4.1 7.7 1.0 CG A:HIS340 4.2 19.7 1.0 CG A:GLU363 4.2 36.6 1.0 ND1 A:HIS340 4.3 26.3 1.0 OE1 A:GLU316 4.3 28.8 1.0 CG A:HIS344 4.3 17.5 1.0 ND1 A:HIS344 4.4 15.7 1.0 CG2 A:THR366 4.5 10.9 1.0 CD A:GLU316 4.7 27.7 1.0 OH A:TYR429 4.7 30.2 1.0 O A:HOH2166 4.8 24.1 1.0 CZ A:TYR429 4.9 22.4 1.0 OE2 A:GLU341 4.9 36.3 1.0 OE2 A:GLU316 4.9 25.1 1.0 CD2 A:TYR429 5.0 21.1 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