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Zinc in PDB 6enc: LTA4 Hydrolase in Complex with COMPOUND11

Enzymatic activity of LTA4 Hydrolase in Complex with COMPOUND11

All present enzymatic activity of LTA4 Hydrolase in Complex with COMPOUND11:
3.3.2.6;

Protein crystallography data

The structure of LTA4 Hydrolase in Complex with COMPOUND11, PDB code: 6enc was solved by H.Srinivas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.18 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.063, 87.175, 99.154, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 19.5

Other elements in 6enc:

The structure of LTA4 Hydrolase in Complex with COMPOUND11 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 COMPOUND11 (pdb code 6enc). 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 COMPOUND11, PDB code: 6enc:

Zinc binding site 1 out of 1 in 6enc

Go back to Zinc Binding Sites List in 6enc
Zinc binding site 1 out of 1 in the LTA4 Hydrolase in Complex with COMPOUND11


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 COMPOUND11 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:30.2
occ:1.00
OE1 A:GLU318 2.1 33.1 1.0
O8 A:BGW707 2.2 3.0 1.0
NE2 A:HIS299 2.2 14.9 1.0
NE2 A:HIS295 2.3 21.4 1.0
O9 A:BGW707 2.6 39.6 1.0
OE2 A:GLU318 2.7 29.2 1.0
CD A:GLU318 2.7 36.1 1.0
C7 A:BGW707 2.7 31.6 1.0
O A:HOH803 2.9 30.0 1.0
CD2 A:HIS295 3.2 20.6 1.0
CD2 A:HIS299 3.2 15.3 1.0
CE1 A:HIS299 3.2 14.4 1.0
CE1 A:HIS295 3.3 21.2 1.0
O A:HOH807 3.5 30.0 1.0
CE2 A:TYR383 3.6 29.5 1.0
OH A:TYR383 3.7 38.0 1.0
CZ A:TYR383 4.1 36.6 1.0
CG A:GLU318 4.1 28.7 1.0
C6 A:BGW707 4.2 38.8 1.0
OE1 A:GLU271 4.3 23.9 1.0
CG A:HIS299 4.4 14.9 1.0
ND1 A:HIS299 4.4 16.0 1.0
CG A:HIS295 4.4 19.4 1.0
ND1 A:HIS295 4.4 21.3 1.0
O A:HOH866 4.5 31.6 1.0
OE2 A:GLU296 4.7 47.4 1.0
CD2 A:TYR383 4.7 27.5 1.0
OE2 A:GLU271 4.7 21.9 1.0
CD A:GLU271 4.8 30.1 1.0
CG2 A:THR321 4.8 12.0 1.0
OE1 A:GLU296 4.8 32.6 1.0
C1 A:BGW707 4.9 43.1 1.0
C5 A:BGW707 4.9 41.6 1.0
CB A:GLU318 5.0 18.5 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 11:43:33 2020

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