Zinc in PDB 8awh: Leukotriene A4 Hydrolase in Complex with 4-(4-Benzylphenyl)-Selenazol- 2-Amine

Enzymatic activity of Leukotriene A4 Hydrolase in Complex with 4-(4-Benzylphenyl)-Selenazol- 2-Amine

All present enzymatic activity of Leukotriene A4 Hydrolase in Complex with 4-(4-Benzylphenyl)-Selenazol- 2-Amine:
3.3.2.6; 3.4.11.4;

Protein crystallography data

The structure of Leukotriene A4 Hydrolase in Complex with 4-(4-Benzylphenyl)-Selenazol- 2-Amine, PDB code: 8awh was solved by T.Teder, J.Z.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.13 / 1.42
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.022, 87.519, 99.007, 90, 90, 90
R / Rfree (%) 15.6 / 18.7

Other elements in 8awh:

The structure of Leukotriene A4 Hydrolase in Complex with 4-(4-Benzylphenyl)-Selenazol- 2-Amine also contains other interesting chemical elements:

Ytterbium (Yb) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Leukotriene A4 Hydrolase in Complex with 4-(4-Benzylphenyl)-Selenazol- 2-Amine (pdb code 8awh). 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 4-(4-Benzylphenyl)-Selenazol- 2-Amine, PDB code: 8awh:

Zinc binding site 1 out of 1 in 8awh

Go back to Zinc Binding Sites List in 8awh
Zinc binding site 1 out of 1 in the Leukotriene A4 Hydrolase in Complex with 4-(4-Benzylphenyl)-Selenazol- 2-Amine


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 4-(4-Benzylphenyl)-Selenazol- 2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:11.5
occ:1.00
 OXT A:ACT705 1.7 12.0 1.0
OE1 A:GLU318 2.0 11.9 1.0
NE2 A:HIS295 2.1 10.8 1.0
NE2 A:HIS299 2.1 9.9 1.0
C A:ACT705 2.4 16.4 1.0
O A:ACT705 2.5 18.4 1.0
CD A:GLU318 2.7 12.4 1.0
OE2 A:GLU318 2.7 13.7 1.0
CD2 A:HIS295 3.0 10.9 1.0
CE1 A:HIS299 3.1 10.6 1.0
CE1 A:HIS295 3.1 10.8 1.0
CD2 A:HIS299 3.1 10.1 1.0
O A:HOH953 3.5 17.5 1.0
CE2 A:TYR383 3.7 14.5 1.0
CH3 A:ACT705 3.9 14.7 1.0
OH A:TYR383 3.9 16.6 1.0
CG A:GLU318 4.1 11.7 1.0
ND1 A:HIS295 4.2 11.0 1.0
ND1 A:HIS299 4.2 10.1 1.0
CG A:HIS295 4.2 10.8 1.0
CG A:HIS299 4.2 10.8 1.0
CZ A:TYR383 4.2 15.6 1.0
OE1 A:GLU271 4.4 12.9 1.0
CG2 A:THR321 4.5 9.4 1.0
CD2 A:TYR383 4.7 13.5 1.0
O A:HOH1030 4.8 14.7 1.0
CB A:GLU318 4.8 11.2 1.0
OE2 A:GLU271 4.9 13.7 1.0
CD A:GLU271 4.9 13.6 1.0
OE2 A:GLU296 4.9 16.1 1.0
CB A:THR321 4.9 9.7 1.0
CA A:GLU318 4.9 11.1 1.0
OE1 A:GLU296 5.0 14.9 1.0

Reference:

T.Teder, S.Konig, R.Singh, B.Samuelsson, O.Werz, U.Garscha, J.Z.Haeggstrom. Modulation of the 5-Lipoxygenase Pathway By Chalcogen-Containing Inhibitors of Leukotriene A4 Hydrolase Int J Mol Sci 2023.
ISSN: ESSN 1422-0067
DOI: 10.3390/IJMS24087539
Page generated: Fri Jul 28 06:29:02 2023

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