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Sodium in PDB 3d4l: Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor
Enzymatic activity of Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor
All present enzymatic activity of Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor:
3.4.14.5;
3.4.14.5;
Protein crystallography data
The structure of Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor, PDB code: 3d4l
was solved by
G.Scapin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 30.00 / 2.00 |
| Space group | P 21 21 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 118.435, 125.749, 137.175, 90.00, 90.00, 90.00 |
| R / Rfree (%) | n/a / n/a |
Other elements in 3d4l:
The structure of Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor also contains other interesting chemical elements:
| Fluorine | (F) | 4 atoms |
Sodium Binding Sites:
The binding sites of Sodium atom in the Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor
(pdb code 3d4l). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor, PDB code: 3d4l:
In total only one binding site of Sodium was determined in the Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor, PDB code: 3d4l:
Sodium binding site 1 out of 1 in 3d4l
Go back to
Sodium Binding Sites List in 3d4l
Sodium binding site 1 out
of 1 in the Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Human Dipeptidyl Peptidase IV/CD26 in Complex with A Novel Inhibitor within 5.0Å range:
|
Reference:
G.B.Liang,
X.Qian,
T.Biftu,
S.Singh,
Y.D.Gao,
G.Scapin,
S.Patel,
B.Leiting,
R.Patel,
J.Wu,
X.Zhang,
N.A.Thornberry,
A.E.Weber.
Discovery of New Binding Elements in Dpp-4 Inhibition and Their Applications in Novel Dpp-4 Inhibitor Design. Bioorg.Med.Chem.Lett. V. 18 3706 2008.
ISSN: ISSN 0960-894X
PubMed: 18524582
DOI: 10.1016/J.BMCL.2008.05.061
Page generated: Mon Oct 7 08:09:42 2024
ISSN: ISSN 0960-894X
PubMed: 18524582
DOI: 10.1016/J.BMCL.2008.05.061
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