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Zinc in PDB 6enb: LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro PeptideEnzymatic 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:
Other elements in 6enb:
The structure of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide also contains other interesting chemical elements:
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 6enbGo 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
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.
Page generated: Wed Dec 16 11:43:33 2020
ISSN: ESSN 2045-2322 PubMed: 29051536 DOI: 10.1038/S41598-017-13490-1 |
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