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Atomistry » Ytterbium » PDB 5l2m-8t0t » 6end | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Ytterbium » PDB 5l2m-8t0t » 6end » |
Ytterbium in PDB 6end: LTA4 Hydrolase in Complex with COMPOUND15Enzymatic 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:
Other elements in 6end:
The structure of LTA4 Hydrolase in Complex with COMPOUND15 also contains other interesting chemical elements:
Ytterbium Binding Sites:
The binding sites of Ytterbium atom in the LTA4 Hydrolase in Complex with COMPOUND15
(pdb code 6end). This binding sites where shown within
5.0 Angstroms radius around Ytterbium atom.
In total 2 binding sites of Ytterbium where determined in the LTA4 Hydrolase in Complex with COMPOUND15, PDB code: 6end: Jump to Ytterbium binding site number: 1; 2; Ytterbium binding site 1 out of 2 in 6endGo back to Ytterbium Binding Sites List in 6end
Ytterbium binding site 1 out
of 2 in the LTA4 Hydrolase in Complex with COMPOUND15
Mono view Stereo pair view
Ytterbium binding site 2 out of 2 in 6endGo back to Ytterbium Binding Sites List in 6end
Ytterbium binding site 2 out
of 2 in the LTA4 Hydrolase in Complex with COMPOUND15
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: Sat Oct 12 21:23:24 2024
ISSN: ESSN 2045-2322 PubMed: 29051536 DOI: 10.1038/S41598-017-13490-1 |
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