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Zinc in PDB 5bpp: Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ

Enzymatic activity of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ

All present enzymatic activity of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ:
3.3.2.6;

Protein crystallography data

The structure of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ, PDB code: 5bpp was solved by J.Huang, N.N.Dong, Q.Xiao, P.Y.Ou, D.Wu, W.Q.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.59 / 2.03
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.983, 87.186, 99.434, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 22.4

Other elements in 5bpp:

The structure of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ also contains other interesting chemical elements:

Ytterbium (Yb) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ (pdb code 5bpp). 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 Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ, PDB code: 5bpp:

Zinc binding site 1 out of 1 in 5bpp

Go back to Zinc Binding Sites List in 5bpp
Zinc binding site 1 out of 1 in the Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor 4AZ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:22.8
occ:1.00
 OE1 A:GLU318 1.9 25.0 1.0
N10 A:A4Z706 2.1 23.5 1.0
NE2 A:HIS299 2.1 17.8 1.0
NE2 A:HIS295 2.2 20.0 1.0
O9 A:A4Z706 2.6 34.2 1.0
OE2 A:GLU318 2.6 23.4 1.0
CD A:GLU318 2.7 20.2 1.0
C8 A:A4Z706 2.7 32.2 1.0
O11 A:A4Z706 3.0 16.7 1.0
CE1 A:HIS299 3.0 18.0 1.0
CE1 A:HIS295 3.1 21.7 1.0
CD2 A:HIS295 3.1 18.6 1.0
CD2 A:HIS299 3.2 15.9 1.0
O A:HOH803 3.4 30.2 1.0
CE2 A:TYR383 3.9 22.1 1.0
C1 A:A4Z706 4.2 36.8 1.0
CG A:GLU318 4.2 20.4 1.0
ND1 A:HIS299 4.2 18.6 1.0
OH A:TYR383 4.2 18.7 1.0
OE1 A:GLU271 4.2 21.3 1.0
ND1 A:HIS295 4.2 19.8 1.0
CG A:HIS295 4.3 20.4 1.0
CG A:HIS299 4.3 17.1 1.0
CZ A:TYR383 4.5 21.9 1.0
CG2 A:THR321 4.5 19.0 1.0
O A:HOH910 4.6 21.6 1.0
OE2 A:GLU271 4.7 19.9 1.0
CD A:GLU271 4.7 19.7 1.0
C2 A:A4Z706 4.8 44.0 1.0
OE1 A:GLU296 4.8 28.7 1.0
CD2 A:TYR383 4.8 20.7 1.0
OE2 A:GLU296 4.8 26.1 1.0
CB A:GLU318 4.9 18.6 1.0
CB A:THR321 4.9 18.5 1.0
CA A:GLU318 5.0 19.4 1.0

Reference:

Q.Xiao, N.N.Dong, X.Yao, D.Wu, Y.Lu, F.Mao, J.Zhu, J.Li, J.Huang, A.Chen, L.Huang, X.Wang, G.Yang, G.He, Y.Xu, W.Q.Lu. Bufexamac Ameliorates Lps-Induced Acute Lung Injury in Mice By Targeting LTA4H Sci Rep V. 6 25298 2016.
ISSN: ESSN 2045-2322
PubMed: 27126280
DOI: 10.1038/SREP25298
Page generated: Sun Oct 27 13:29:39 2024

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