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Zinc in PDB 3ftx: Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin

Enzymatic activity of Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin

All present enzymatic activity of Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin:
3.3.2.6;

Protein crystallography data

The structure of Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin, PDB code: 3ftx was solved by D.R.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.96
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.476, 86.995, 99.703, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 21

Other elements in 3ftx:

The structure of Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin also contains other interesting chemical elements:

Ytterbium (Yb) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin (pdb code 3ftx). 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 Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin, PDB code: 3ftx:

Zinc binding site 1 out of 1 in 3ftx

Go back to Zinc Binding Sites List in 3ftx
Zinc binding site 1 out of 1 in the Leukotriene A4 Hydrolase in Complex with Dihydroresveratrol and Bestatin


Mono view


Stereo pair view

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

b:16.1
occ:1.00
 NE2 A:HIS295 2.0 11.9 1.0
NE2 A:HIS299 2.1 11.0 1.0
O2 A:BES720 2.1 16.0 1.0
OE1 A:GLU318 2.2 16.0 1.0
OE2 A:GLU318 2.5 11.5 1.0
O3 A:BES720 2.6 18.9 1.0
CD A:GLU318 2.7 13.8 1.0
CD2 A:HIS295 3.0 10.0 1.0
CD2 A:HIS299 3.0 6.3 1.0
C2 A:BES720 3.0 17.2 1.0
CE1 A:HIS295 3.0 11.3 1.0
C3 A:BES720 3.1 19.3 1.0
CE1 A:HIS299 3.1 7.2 1.0
C1 A:BES720 3.6 16.0 1.0
OE1 A:GLU296 4.0 13.9 1.0
CE2 A:TYR383 4.1 16.1 1.0
N2 A:BES720 4.1 16.0 1.0
ND1 A:HIS295 4.1 12.9 1.0
CG A:HIS295 4.1 11.8 1.0
CG A:HIS299 4.2 9.1 1.0
ND1 A:HIS299 4.2 8.6 1.0
CG A:GLU318 4.2 12.7 1.0
N1 A:BES720 4.3 18.0 1.0
OE1 A:GLU271 4.3 8.7 1.0
CG2 A:THR321 4.4 10.2 1.0
OH A:TYR383 4.4 12.6 1.0
O A:HOH792 4.5 21.7 1.0
OE2 A:GLU296 4.7 10.2 1.0
CZ A:TYR383 4.7 13.5 1.0
CD A:GLU271 4.7 9.5 1.0
CD A:GLU296 4.7 12.3 1.0
OE2 A:GLU271 4.8 11.7 1.0
CB A:THR321 4.8 10.4 1.0
CB A:GLU318 4.9 12.9 1.0
C6 A:BES720 5.0 15.4 1.0

Reference:

D.R.Davies, B.Mamat, O.T.Magnusson, J.Christensen, M.H.Haraldsson, R.Mishra, B.Pease, E.Hansen, J.Singh, D.Zembower, H.Kim, A.S.Kiselyov, A.B.Burgin, M.E.Gurney, L.J.Stewart. Discovery of Leukotriene A4 Hydrolase Inhibitors Using Metabolomics Biased Fragment Crystallography. J.Med.Chem. V. 52 4694 2009.
ISSN: ISSN 0022-2623
PubMed: 19618939
DOI: 10.1021/JM900259H
Page generated: Thu Oct 24 13:24:36 2024

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