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Zinc in PDB 2xpy: Structure of Native Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae

Enzymatic activity of Structure of Native Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae

All present enzymatic activity of Structure of Native Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae:
3.3.2.6;

Protein crystallography data

The structure of Structure of Native Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae, PDB code: 2xpy 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) 26.01 / 2.73
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 159.556, 159.556, 76.832, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 24

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Native Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae (pdb code 2xpy). 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 Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae, PDB code: 2xpy:

Zinc binding site 1 out of 1 in 2xpy

Go back to Zinc Binding Sites List in 2xpy
Zinc binding site 1 out of 1 in the Structure of Native Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae


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 Leukotriene A4 Hydrolase From Saccharomyces Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1673

b:29.2
occ:1.00
NE2 A:HIS344 2.1 29.2 1.0
NE2 A:HIS340 2.1 20.6 1.0
OE1 A:GLU363 2.1 23.5 1.0
OE2 A:GLU363 2.4 44.0 1.0
O A:HOH2113 2.5 23.8 1.0
CD A:GLU363 2.6 30.4 1.0
O A:HOH2112 2.8 23.6 1.0
CD2 A:HIS340 3.0 17.9 1.0
CE1 A:HIS344 3.0 28.5 1.0
CD2 A:HIS344 3.1 31.1 1.0
CE1 A:HIS340 3.2 19.9 1.0
OE1 A:GLU316 3.9 37.6 1.0
CG A:GLU363 4.1 19.4 1.0
CE2 A:TYR429 4.1 36.9 1.0
ND1 A:HIS344 4.2 29.1 1.0
CG A:HIS340 4.2 25.2 1.0
CG A:HIS344 4.2 29.4 1.0
ND1 A:HIS340 4.2 28.6 1.0
OH A:TYR429 4.3 42.3 1.0
CD A:GLU316 4.6 32.5 1.0
CG2 A:THR366 4.6 14.2 1.0
CZ A:TYR429 4.7 35.3 1.0
OE2 A:GLU316 4.8 35.2 1.0
CB A:GLU363 4.9 25.0 1.0
CB A:THR366 4.9 21.6 1.0

Reference:

C.Helgstrand, M.Hasan, H.Uysal, J.Z.Haeggstr, 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
Page generated: Wed Aug 20 06:49:53 2025

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