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Zinc in PDB 6end: LTA4 Hydrolase in Complex with COMPOUND15

Enzymatic activity of LTA4 Hydrolase in Complex with COMPOUND15

All present enzymatic activity of LTA4 Hydrolase in Complex with COMPOUND15:
3.3.2.6;

Protein crystallography data

The structure of LTA4 Hydrolase in Complex with COMPOUND15, PDB code: 6end was solved by H.Srinivas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.33 / 2.24
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.410, 87.135, 99.580, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 21.7

Other elements in 6end:

The structure of LTA4 Hydrolase in Complex with COMPOUND15 also contains other interesting chemical elements:

Ytterbium (Yb) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the LTA4 Hydrolase in Complex with COMPOUND15 (pdb code 6end). 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 LTA4 Hydrolase in Complex with COMPOUND15, PDB code: 6end:

Zinc binding site 1 out of 1 in 6end

Go back to Zinc Binding Sites List in 6end
Zinc binding site 1 out of 1 in the LTA4 Hydrolase in Complex with COMPOUND15


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of LTA4 Hydrolase in Complex with COMPOUND15 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:21.7
occ:1.00
OE1 A:GLU318 2.2 31.9 1.0
NE2 A:HIS299 2.2 14.7 1.0
NE2 A:HIS295 2.2 15.2 1.0
OE2 A:GLU318 2.6 33.6 1.0
CD A:GLU318 2.7 38.2 1.0
O A:HOH943 2.7 33.6 1.0
O A:HOH1055 3.1 39.7 1.0
CE1 A:HIS299 3.2 14.3 1.0
CD2 A:HIS295 3.2 15.0 1.0
CE1 A:HIS295 3.2 14.7 1.0
CD2 A:HIS299 3.2 14.1 1.0
O A:HOH825 3.5 23.6 1.0
CE2 A:TYR383 3.7 25.1 1.0
OH A:TYR383 3.8 36.0 1.0
CG A:GLU318 4.1 32.9 1.0
CZ A:TYR383 4.2 33.7 1.0
OE1 A:GLU271 4.2 33.3 1.0
ND1 A:HIS299 4.3 15.2 1.0
CG A:HIS299 4.3 13.2 1.0
CG A:HIS295 4.3 14.1 1.0
ND1 A:HIS295 4.4 15.4 1.0
OE2 A:GLU271 4.6 21.5 1.0
CG2 A:THR321 4.7 7.8 1.0
CD A:GLU271 4.7 28.9 1.0
CD2 A:TYR383 4.7 23.8 1.0
OE2 A:GLU296 4.8 32.1 1.0
O A:HOH876 4.8 37.1 1.0
OE1 A:GLU296 4.9 25.0 1.0

Reference:

S.Numao, F.Hasler, C.Laguerre, H.Srinivas, N.Wack, P.Jager, A.Schmid, A.Osmont, P.Rothlisberger, J.Houguenade, C.Bergsdorf, J.Dawson, N.Carte, A.Hofmann, C.Markert, L.Hardaker, A.Billich, R.M.Wolf, C.A.Penno, B.Bollbuck, W.Miltz, T.A.Rohn. Feasibility and Physiological Relevance of Designing Highly Potent Aminopeptidase-Sparing Leukotriene A4 Hydrolase Inhibitors. Sci Rep V. 7 13591 2017.
ISSN: ESSN 2045-2322
PubMed: 29051536
DOI: 10.1038/S41598-017-13490-1
Page generated: Wed Dec 16 11:43:36 2020

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