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Zinc in PDB 6enb: LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide

Enzymatic activity of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide

All present enzymatic activity of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide:
3.3.2.6;

Protein crystallography data

The structure of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide, PDB code: 6enb was solved by H.Srinivas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.01 / 1.84
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.443, 87.576, 99.058, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 18.6

Other elements in 6enb:

The structure of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide also contains other interesting chemical elements:

Ytterbium (Yb) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide (pdb code 6enb). 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 (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide, PDB code: 6enb:

Zinc binding site 1 out of 1 in 6enb

Go back to Zinc Binding Sites List in 6enb
Zinc binding site 1 out of 1 in the LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:18.3
occ:1.00
 OE1 A:GLU318 2.1 26.5 1.0
NE2 A:HIS295 2.3 19.3 1.0
C B:PRO1 2.4 56.1 1.0
NE2 A:HIS299 2.4 18.6 1.0
O B:PRO1 2.5 53.8 1.0
CA B:PRO1 2.6 54.4 1.0
CD A:GLU318 2.7 28.2 1.0
N B:PRO1 2.7 54.5 1.0
OE2 A:GLU318 2.7 29.6 1.0
N B:GLY2 3.0 51.8 1.0
CD2 A:HIS295 3.3 19.5 1.0
CE1 A:HIS295 3.3 19.1 1.0
CE1 A:HIS299 3.4 17.8 1.0
CD2 A:HIS299 3.4 18.5 1.0
CE2 A:TYR383 3.8 29.1 1.0
OH A:TYR383 3.8 33.0 1.0
CA B:GLY2 3.9 50.7 1.0
CG A:GLU318 4.1 25.8 1.0
OE1 A:GLU271 4.2 22.8 1.0
CB B:PRO1 4.2 56.1 1.0
CD B:PRO1 4.2 55.9 1.0
CZ A:TYR383 4.2 33.8 1.0
CG A:HIS295 4.4 18.1 1.0
ND1 A:HIS295 4.5 20.1 1.0
ND1 A:HIS299 4.5 19.4 1.0
CG A:HIS299 4.6 17.8 1.0
O A:HOH846 4.6 25.4 1.0
OE2 A:GLU271 4.7 21.0 1.0
CD A:GLU271 4.7 26.1 1.0
NE2 A:GLN296 4.8 15.8 1.0
CG B:PRO1 4.8 60.4 1.0
CD2 A:TYR383 4.9 27.7 1.0
CB A:GLU318 5.0 17.2 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: Mon Oct 28 20:14:12 2024

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