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Zinc in PDB 3ftz: Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline

Enzymatic activity of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline

All present enzymatic activity of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline:
3.3.2.6;

Protein crystallography data

The structure of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline, PDB code: 3ftz 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 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.200, 87.094, 99.405, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 22.3

Other elements in 3ftz:

The structure of Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline also contains other interesting chemical elements:

Ytterbium (Yb) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline (pdb code 3ftz). 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 Fragment 2-(Pyridin-3- Ylmethoxy)Aniline, PDB code: 3ftz:

Zinc binding site 1 out of 1 in 3ftz

Go back to Zinc Binding Sites List in 3ftz
Zinc binding site 1 out of 1 in the Leukotriene A4 Hydrolase in Complex with Fragment 2-(Pyridin-3- Ylmethoxy)Aniline


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 Fragment 2-(Pyridin-3- Ylmethoxy)Aniline within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:25.2
occ:1.00
 OE1 A:GLU318 2.0 22.1 1.0
NE2 A:HIS299 2.1 15.9 1.0
OXT A:ACT803 2.1 33.4 1.0
NE2 A:HIS295 2.1 17.2 1.0
CD A:GLU318 2.7 20.1 1.0
OE2 A:GLU318 2.7 19.9 1.0
O A:ACT803 2.8 33.0 1.0
C A:ACT803 2.9 33.3 1.0
CE1 A:HIS299 3.0 15.1 1.0
CE1 A:HIS295 3.1 17.8 1.0
CD2 A:HIS299 3.1 15.0 1.0
CD2 A:HIS295 3.1 15.1 1.0
CE2 A:TYR383 3.7 20.1 1.0
O A:HOH852 3.8 18.9 1.0
OH A:TYR383 4.1 19.2 1.0
ND1 A:HIS299 4.1 15.4 1.0
ND1 A:HIS295 4.2 16.6 1.0
CG A:GLU318 4.2 19.6 1.0
CG A:HIS299 4.2 15.7 1.0
CG A:HIS295 4.2 16.2 1.0
CH3 A:ACT803 4.3 33.0 1.0
CZ A:TYR383 4.3 20.4 1.0
CG2 A:THR321 4.4 16.6 1.0
OE1 A:GLU271 4.4 17.7 1.0
CD2 A:TYR383 4.6 16.3 1.0
CB A:THR321 4.7 16.9 1.0
O A:HOH663 4.7 16.3 1.0
CB A:GLU318 4.8 19.5 1.0
CA A:GLU318 4.8 19.4 1.0
CD A:GLU271 4.9 19.2 1.0
OE2 A:GLU296 4.9 20.2 1.0
OE2 A:GLU271 4.9 19.8 1.0

Reference:

V.Sandanayaka, B.Mamat, R.K.Mishra, J.Winger, M.Krohn, L.M.Zhou, M.Keyvan, L.Enache, D.Sullins, E.Onua, J.Zhang, G.Halldorsdottir, H.Sigthorsdottir, A.Thorlaksdottir, G.Sigthorsson, M.Thorsteinnsdottir, D.R.Davies, L.J.Stewart, D.E.Zembower, T.Andresson, A.S.Kiselyov, J.Singh, M.E.Gurney. Discovery of 4-[(2S)-2-{[4-(4-Chlorophenoxy)Phenoxy]Methyl}-1- Pyrrolidinyl]Butanoic Acid (Dg-051) As A Novel Leukotriene A4 Hydrolase Inhibitor of Leukotriene B4 Biosynthesis. J.Med.Chem. V. 53 573 2010.
ISSN: ISSN 0022-2623
PubMed: 19950900
DOI: 10.1021/JM900838G
Page generated: Thu Oct 24 13:24:54 2024

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